JMJD6 cleaves MePCE to release positive transcription elongation factor b (P-TEFb) in higher eukaryotes
More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechan...
Saved in:
Published in | eLife Vol. 9 |
---|---|
Main Authors | , , , , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
eLife Science Publications, Ltd
12.02.2020
eLife Sciences Publications Ltd eLife Sciences Publications, Ltd |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)'s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of
knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. |
---|---|
AbstractList | More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)'s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of
knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)'s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of Jmjd6 knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)’s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of Jmjd6 knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. In animals, an enzyme known as RNA polymerase II (Pol II for short) is a key element of the transcription process, whereby the genetic information contained in DNA is turned into messenger RNA molecules in the cells, which can then be translated to proteins. To perform this task, Pol II needs to be activated by a complex of proteins called P-TEFb; however, P-TEFb is usually found in an inactive form held by another group of proteins. Yet, it is unclear how P-TEFb is released and allowed to activate Pol II. Scientists have speculated that another protein called JMJD6 (Jumonji domain-containing 6) is important for P-TEFb to activate Pol II. Various roles for JMJD6 have been proposed, but its exact purpose remains unclear. Recently, two enzymes closely related to JMJD6 were found to be able to make precise cuts in other proteins; Lee, Liu et al. therefore wanted to test whether this is also true of JMJD6. Experiments using purified JMJD6 showed that it could make a cut in an enzyme called MePCE, which belongs to the group of proteins that hold P-TEFb in its inactive form. Lee, Liu et al. then tested the relationships between these proteins in living human and mouse cells. The levels of activated Pol II were lower in cells without JMJD6 and higher in those without MePCE. Together, the results suggest that JMJD6 cuts MePCE to release P-TEFb, which then activates Pol II. JMJD6 appears to know where to cut by following a specific pattern of elements in the structure of MePCE. When MePCE was mutated so that the pattern changed, JMJD6 was unable to cut it. These results suggest that JMJD6 and related enzymes belong to a new family of proteases, the molecular scissors that can cleave other proteins. The molecules that regulate transcription often are major drug targets, for example in the fight against cancer. Ultimately, understanding the role of JMJD6 might help to identify new avenues for cancer drug development. More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)'s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of Jmjd6 knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. eLife digest In animals, an enzyme known as RNA polymerase II (Pol II for short) is a key element of the transcription process, whereby the genetic information contained in DNA is turned into messenger RNA molecules in the cells, which can then be translated to proteins. To perform this task, Pol II needs to be activated by a complex of proteins called P-TEFb; however, P-TEFb is usually found in an inactive form held by another group of proteins. Yet, it is unclear how P-TEFb is released and allowed to activate Pol II. Scientists have speculated that another protein called JMJD6 (Jumonji domain-containing 6) is important for P-TEFb to activate Pol II. Various roles for JMJD6 have been proposed, but its exact purpose remains unclear. Recently, two enzymes closely related to JMJD6 were found to be able to make precise cuts in other proteins; Lee, Liu et al. therefore wanted to test whether this is also true of JMJD6. Experiments using purified JMJD6 showed that it could make a cut in an enzyme called MePCE, which belongs to the group of proteins that hold P-TEFb in its inactive form. Lee, Liu et al. then tested the relationships between these proteins in living human and mouse cells. The levels of activated Pol II were lower in cells without JMJD6 and higher in those without MePCE. Together, the results suggest that JMJD6 cuts MePCE to release P-TEFb, which then activates Pol II. JMJD6 appears to know where to cut by following a specific pattern of elements in the structure of MePCE. When MePCE was mutated so that the pattern changed, JMJD6 was unable to cut it. These results suggest that JMJD6 and related enzymes belong to a new family of proteases, the molecular scissors that can cleave other proteins. The molecules that regulate transcription often are major drug targets, for example in the fight against cancer. Ultimately, understanding the role of JMJD6 might help to identify new avenues for cancer drug development. More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. The exact mechanism on how the sequestered P-TEFb is released from the 7SK snRNP complex and recruited to Pol II CTD remains unknown. In this report, we utilize mouse and human models to reveal methylphosphate capping enzyme (MePCE), a core component of the 7SK snRNP complex, as the cognate substrate for Jumonji domain-containing 6 (JMJD6)’s novel proteolytic function. Our evidences consist of a crystal structure of JMJD6 bound to methyl-arginine, enzymatic assays of JMJD6 cleaving MePCE in vivo and in vitro, binding assays, and downstream effects of Jmjd6 knockout and overexpression on Pol II CTD phosphorylation. We propose that JMJD6 assists bromodomain containing 4 (BRD4) to recruit P-TEFb to Pol II CTD by disrupting the 7SK snRNP complex. In animals, an enzyme known as RNA polymerase II (Pol II for short) is a key element of the transcription process, whereby the genetic information contained in DNA is turned into messenger RNA molecules in the cells, which can then be translated to proteins. To perform this task, Pol II needs to be activated by a complex of proteins called P-TEFb; however, P-TEFb is usually found in an inactive form held by another group of proteins. Yet, it is unclear how P-TEFb is released and allowed to activate Pol II. Scientists have speculated that another protein called JMJD6 (Jumonji domain-containing 6) is important for P-TEFb to activate Pol II. Various roles for JMJD6 have been proposed, but its exact purpose remains unclear. Recently, two enzymes closely related to JMJD6 were found to be able to make precise cuts in other proteins; Lee, Liu et al. therefore wanted to test whether this is also true of JMJD6. Experiments using purified JMJD6 showed that it could make a cut in an enzyme called MePCE, which belongs to the group of proteins that hold P-TEFb in its inactive form. Lee, Liu et al. then tested the relationships between these proteins in living human and mouse cells. The levels of activated Pol II were lower in cells without JMJD6 and higher in those without MePCE. Together, the results suggest that JMJD6 cuts MePCE to release P-TEFb, which then activates Pol II. JMJD6 appears to know where to cut by following a specific pattern of elements in the structure of MePCE. When MePCE was mutated so that the pattern changed, JMJD6 was unable to cut it. These results suggest that JMJD6 and related enzymes belong to a new family of proteases, the molecular scissors that can cleave other proteins. The molecules that regulate transcription often are major drug targets, for example in the fight against cancer. Ultimately, understanding the role of JMJD6 might help to identify new avenues for cancer drug development. |
Audience | Academic |
Author | Bernt, Kathrin Maria Liu, Haolin Liu, Xinjian Crawford, Fran Chen, Zhongzhou Hill, Ryan Lee, Schuyler Hong, Xia Li, Chuan-Yuan Chen, Chunjing Marrack, Philippa Kingsley, Molly Zhang, Qianqian Lengeling, Andreas Hansen, Kirk Xue, Yuhua Kappler, John Zhou, Qiang Zhang, Gongyi |
Author_xml | – sequence: 1 givenname: Schuyler orcidid: 0000-0003-4623-4075 surname: Lee fullname: Lee, Schuyler organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States – sequence: 2 givenname: Haolin surname: Liu fullname: Liu, Haolin organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States – sequence: 3 givenname: Ryan surname: Hill fullname: Hill, Ryan organization: Department of Genetics and Biochemistry, School of Medicine, University of Colorado, Aurora, United States – sequence: 4 givenname: Chunjing surname: Chen fullname: Chen, Chunjing organization: State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Xiamen University, Xiamen, China – sequence: 5 givenname: Xia surname: Hong fullname: Hong, Xia organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States – sequence: 6 givenname: Fran surname: Crawford fullname: Crawford, Fran organization: Department of Biomedical Research, National Jewish Health, Denver, United States – sequence: 7 givenname: Molly orcidid: 0000-0002-5921-3743 surname: Kingsley fullname: Kingsley, Molly organization: Department of Pediatrics and the Center for Childhood Cancer Research, Children's Hospital of Philadelphia, Philadelphia, United States – sequence: 8 givenname: Qianqian surname: Zhang fullname: Zhang, Qianqian organization: State Key Laboratory of Agrobiotechnology, China Agriculture University, Beijing, China – sequence: 9 givenname: Xinjian surname: Liu fullname: Liu, Xinjian organization: Department of Dermatology, Duke University, Durham, United States – sequence: 10 givenname: Zhongzhou surname: Chen fullname: Chen, Zhongzhou organization: State Key Laboratory of Agrobiotechnology, China Agriculture University, Beijing, China – sequence: 11 givenname: Andreas surname: Lengeling fullname: Lengeling, Andreas organization: Max-Planck-Society, Administrative Headquarters, Munich, Germany – sequence: 12 givenname: Kathrin Maria orcidid: 0000-0002-0691-356X surname: Bernt fullname: Bernt, Kathrin Maria organization: Department of Molecular and Cell Biology, University of California, Berkeley, United States – sequence: 13 givenname: Philippa orcidid: 0000-0003-1883-3687 surname: Marrack fullname: Marrack, Philippa organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States – sequence: 14 givenname: John surname: Kappler fullname: Kappler, John organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States – sequence: 15 givenname: Qiang orcidid: 0000-0001-7202-3947 surname: Zhou fullname: Zhou, Qiang organization: Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States – sequence: 16 givenname: Chuan-Yuan orcidid: 0000-0002-0418-6231 surname: Li fullname: Li, Chuan-Yuan organization: Department of Dermatology, Duke University, Durham, United States – sequence: 17 givenname: Yuhua surname: Xue fullname: Xue, Yuhua organization: State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Xiamen University, Xiamen, China – sequence: 18 givenname: Kirk surname: Hansen fullname: Hansen, Kirk organization: Department of Genetics and Biochemistry, School of Medicine, University of Colorado, Aurora, United States – sequence: 19 givenname: Gongyi orcidid: 0000-0003-3010-3804 surname: Zhang fullname: Zhang, Gongyi organization: Department of Immunology and Microbiology, School of Medicine, University of Colorado, Aurora, United States |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32048991$$D View this record in MEDLINE/PubMed |
BookMark | eNptksFv0zAUhyM0xMbYiTuyxGUTarFjx3EuSFPpoFMnJhgSN8txXlKX1C62U8F_j9uOsSKSQ6znz5_tl9_z7Mg6C1n2kuBxWRTsLcxNC-OCVhQ_yU5yXOARFuzb0aPxcXYWwhKnp2RCkOpZdkxzzERVkZOsu765fs-R7kFtIKAbuJ1MUXTIQ6oEQGsXTDQbQNErG7Q362icRdA726ndsFU6Oo9qdH47upte1RfIWLQw3QI8guG78r9chPAie9qqPsDZ_fc0-3o1vZt8HM0_fZhNLucjzYmIo1bVpKkawXMNutK8oJjhkhNNmFJljWmTC1y1OavrNK8E4QxzQRgFRYmmnJ5ms723cWop196s0gGkU0buCs53Uvlo0n1lSyoBgnEooWWaN8nYUC0qpnOelzvXu71rPdQraDTY1IT-QHo4Y81Cdm4jS8wZZUUSnN8LvPsxQIhyZYKGvlcW3BBkTgtGyoIW271e_4Mu3eBtalWiBCsZSX_uL9WpdAFjW5f21VupvOSEVwUuy61r_B8qvQ2sjE75aU2qHyy4OFiQmAg_Y6eGEOTsy-dD9s2e1d6F4KF96AfBchtJuYuk3EUy0a8et_CB_RNA-htbudtX |
CitedBy_id | crossref_primary_10_1042_BST20221147 crossref_primary_10_1016_j_tig_2020_09_013 crossref_primary_10_1002_wrna_1782 crossref_primary_10_1073_pnas_2200753119 crossref_primary_10_3390_biom12030347 crossref_primary_10_3390_ijms24010460 crossref_primary_10_1002_ctm2_328 crossref_primary_10_1002_ar_25203 crossref_primary_10_3389_fmolb_2023_1154622 crossref_primary_10_3390_ijms21186618 crossref_primary_10_3390_pharmaceutics14010010 crossref_primary_10_1016_j_tibs_2024_06_009 crossref_primary_10_1073_pnas_2005745117 crossref_primary_10_1007_s00018_021_03878_8 crossref_primary_10_1128_mbio_01925_23 crossref_primary_10_1093_genetics_iyad203 crossref_primary_10_3389_fmolb_2021_728777 crossref_primary_10_2174_0113894501269090231012090351 crossref_primary_10_1002_mc_23204 crossref_primary_10_1126_sciadv_adj9359 |
Cites_doi | 10.1128/MCB.01020-07 10.1016/j.cell.2016.10.049 10.1186/1471-2121-5-26 10.1016/S0092-8674(00)81515-9 10.1038/35011084 10.1016/j.bbrc.2012.02.115 10.1016/S0092-8674(00)80939-3 10.1016/j.molcel.2007.06.027 10.1038/s41598-018-21432-8 10.1038/s41598-019-49032-0 10.1038/386569a0 10.1073/pnas.0704525104 10.1242/dev.074138 10.1038/nmeth.2397 10.1002/wrna.106 10.1016/j.cell.2006.03.028 10.1126/science.1087621 10.7554/eLife.02375 10.1038/nature14102 10.1038/s41598-017-16588-8 10.1016/j.yexcr.2003.09.023 10.1101/gad.325142.119 10.1016/j.molcel.2005.06.027 10.1016/j.chembiol.2017.03.004 10.1002/jcb.24035 10.1016/j.ydbio.2011.01.017 10.15252/embr.201743892 10.1093/nar/gku449 10.1093/nar/gkp977 10.1146/annurev-biochem-052610-095910 10.1016/j.cell.2006.04.024 10.1038/nrm3953 10.1016/j.celrep.2018.01.028 10.1002/prot.22570 10.1038/nature09131 10.3390/biom7020041 10.1016/j.molcel.2005.06.029 10.1371/journal.pone.0013769 10.1038/ncomms6717 10.1073/pnas.1706831114 10.1093/nar/gkw585 10.1126/science.1181421 10.1126/science.1175865 10.1074/jbc.R700001200 10.1126/science.1145801 10.1016/j.molcel.2014.02.014 10.1126/science.1162228 10.1073/pnas.1008832107 10.1186/jbiol10 10.1016/j.cell.2013.10.056 10.1038/369151a0 10.1101/gad.2005511 10.1128/MCB.01341-10 |
ContentType | Journal Article |
Copyright | 2020, Lee et al. COPYRIGHT 2020 eLife Science Publications, Ltd. 2020, Lee et al. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2020, Lee et al 2020 Lee et al |
Copyright_xml | – notice: 2020, Lee et al. – notice: COPYRIGHT 2020 eLife Science Publications, Ltd. – notice: 2020, Lee et al. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2020, Lee et al 2020 Lee et al |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION ISR 3V. 7X7 7XB 88E 88I 8FE 8FH 8FI 8FJ 8FK ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO FYUFA GHDGH GNUQQ HCIFZ K9. LK8 M0S M1P M2P M7P PIMPY PQEST PQQKQ PQUKI PRINS Q9U 7X8 5PM DOA |
DOI | 10.7554/eLife.53930 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Gale In Context: Science ProQuest Central (Corporate) ProQuest Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Science Database (Alumni Edition) ProQuest SciTech Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest Central ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection ProQuest One Community College ProQuest Central Korea Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Biological Sciences Health & Medical Collection (Alumni Edition) Medical Database ProQuest Science Journals Biological Science Database Publicly Available Content Database ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China ProQuest Central Basic MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Publicly Available Content Database ProQuest Central Student ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection ProQuest Central China ProQuest Central Health Research Premium Collection Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest Medical Library (Alumni) ProQuest Science Journals (Alumni Edition) ProQuest Biological Science Collection ProQuest Central Basic ProQuest Science Journals ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ProQuest One Academic ProQuest Central (Alumni) MEDLINE - Academic |
DatabaseTitleList | MEDLINE CrossRef Publicly Available Content Database |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
EISSN | 2050-084X |
ExternalDocumentID | oai_doaj_org_article_f198e846e7ef4c6dbecd3c894c262736 A616950776 10_7554_eLife_53930 32048991 |
Genre | Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIAID NIH HHS grantid: T32 AI007405 – fundername: NIAID NIH HHS grantid: T32 AI074491 – fundername: NCI NIH HHS grantid: R01 CA201230 – fundername: NIH HHS grantid: 5T32AI074491-07 – fundername: ; grantid: 5T32AI074491-07 – fundername: ; grantid: CA201230 – fundername: ; grantid: T32AI007405-28 |
GroupedDBID | 3V. 53G 5VS 7X7 88E 88I 8FE 8FH 8FI 8FJ AAFWJ AAKDD ABUWG ACGFO ACGOD ACPRK ADBBV ADRAZ AENEX AFKRA AFPKN ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS AZQEC BAWUL BBNVY BCNDV BENPR BHPHI BPHCQ BVXVI CCPQU CGR CUY CVF DIK DWQXO ECM EIF EMOBN FRP FYUFA GNUQQ GROUPED_DOAJ GX1 HCIFZ HMCUK HYE IAO IEA IHR INH INR ISR ITC KQ8 LK8 M1P M2P M48 M7P M~E NPM NQS OK1 PGMZT PIMPY PQQKQ PROAC PSQYO RHF RHI RNS RPM UKHRP AAYXX CITATION 7XB 8FK K9. PQEST PQUKI PRINS Q9U 7X8 5PM |
ID | FETCH-LOGICAL-c618t-fab1d9d862cec9c653040761c14aa7b03d2809f24bbec9a8164068143ea31c363 |
IEDL.DBID | RPM |
ISSN | 2050-084X |
IngestDate | Fri Oct 04 12:36:15 EDT 2024 Tue Sep 17 20:56:15 EDT 2024 Fri Aug 16 22:19:04 EDT 2024 Fri Sep 13 01:58:23 EDT 2024 Thu Feb 22 23:48:26 EST 2024 Fri Feb 02 04:15:12 EST 2024 Thu Aug 01 20:08:39 EDT 2024 Fri Aug 23 04:01:42 EDT 2024 Sat Sep 28 08:28:19 EDT 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | CDK9 mouse 7SK snRNP chemical biology MePCE biochemistry RNA polymerase II JMJD6 P-TEFb |
Language | English |
License | 2020, Lee et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c618t-fab1d9d862cec9c653040761c14aa7b03d2809f24bbec9a8164068143ea31c363 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work. |
ORCID | 0000-0001-7202-3947 0000-0003-4623-4075 0000-0002-0691-356X 0000-0003-1883-3687 0000-0002-0418-6231 0000-0003-3010-3804 0000-0002-5921-3743 |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7064345/ |
PMID | 32048991 |
PQID | 2384741819 |
PQPubID | 2045579 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_f198e846e7ef4c6dbecd3c894c262736 pubmedcentral_primary_oai_pubmedcentral_nih_gov_7064345 proquest_miscellaneous_2354175356 proquest_journals_2384741819 gale_infotracmisc_A616950776 gale_infotracacademiconefile_A616950776 gale_incontextgauss_ISR_A616950776 crossref_primary_10_7554_eLife_53930 pubmed_primary_32048991 |
PublicationCentury | 2000 |
PublicationDate | 2020-02-12 |
PublicationDateYYYYMMDD | 2020-02-12 |
PublicationDate_xml | – month: 02 year: 2020 text: 2020-02-12 day: 12 |
PublicationDecade | 2020 |
PublicationPlace | England |
PublicationPlace_xml | – name: England – name: Cambridge |
PublicationTitle | eLife |
PublicationTitleAlternate | Elife |
PublicationYear | 2020 |
Publisher | eLife Science Publications, Ltd eLife Sciences Publications Ltd eLife Sciences Publications, Ltd |
Publisher_xml | – name: eLife Science Publications, Ltd – name: eLife Sciences Publications Ltd – name: eLife Sciences Publications, Ltd |
References | Krieger (bib21) 2009; 77 Vangimalla (bib40) 2017; 7 Lee (bib22) 2017; 24 Chang (bib3) 2007; 318 Voong (bib41) 2016; 167 Chen (bib4) 2006; 125 Yang (bib49) 2005; 19 Hahn (bib11) 2010; 5 Wu (bib47) 2007; 282 Itzen (bib15) 2014; 42 Ptashne (bib32) 1997; 386 Shelton (bib36) 2018; 22 Whetstine (bib46) 2006; 125 Ishimura (bib14) 2012; 139 Konuma (bib19) 2017; 7 Oh (bib30) 2012; 420 Zhang (bib52) 1999; 98 Zhou (bib53) 2012; 81 Webby (bib42) 2009; 325 Jang (bib16) 2005; 19 Han (bib12) 2012; 113 Core (bib8) 2019; 33 Jeronimo (bib17) 2007; 27 Shen (bib37) 2017; 18 Schulze-Gahmen (bib35) 2014; 3 Weber (bib43) 2014; 53 Xue (bib48) 2010; 38 Wei (bib44) 1998; 92 Cui (bib9) 2004; 293 Singh (bib38) 2011; 352 Nechaev (bib28) 2010; 327 Liu (bib26) 2018; 8 Cikala (bib6) 2004; 5 Core (bib7) 2008; 322 Kozono (bib20) 1994; 369 Böse (bib1) 2004; 3 Min (bib27) 2011; 25 Rahman (bib33) 2011; 31 Yang (bib51) 2015; 6 Jonkers (bib18) 2015; 16 Liu (bib24) 2013; 155 Fadok (bib10) 2000; 405 Peterlin (bib31) 2012; 3 Hong (bib13) 2010; 107 C Quaresma (bib2) 2016; 44 Chen (bib5) 2007; 104 Yang (bib50) 2008; 28 Neumann (bib29) 2015; 517 Li (bib23) 2003; 302 Tahirov (bib39) 2010; 465 Liu (bib25) 2017; 114 Schneeberger (bib34) 2019; 9 Weimann (bib45) 2013; 10 |
References_xml | – volume: 28 start-page: 967 year: 2008 ident: bib50 article-title: Brd4 recruits P-TEFb to chromosomes at late mitosis to promote G1 gene expression and cell cycle progression publication-title: Molecular and Cellular Biology doi: 10.1128/MCB.01020-07 contributor: fullname: Yang – volume: 167 start-page: 1555 year: 2016 ident: bib41 article-title: Insights into nucleosome organization in mouse embryonic stem cells through chemical mapping publication-title: Cell doi: 10.1016/j.cell.2016.10.049 contributor: fullname: Voong – volume: 5 year: 2004 ident: bib6 article-title: The phosphatidylserine receptor from Hydra is a nuclear protein with potential fe(II) dependent oxygenase activity publication-title: BMC Cell Biology doi: 10.1186/1471-2121-5-26 contributor: fullname: Cikala – volume: 98 start-page: 811 year: 1999 ident: bib52 article-title: Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution publication-title: Cell doi: 10.1016/S0092-8674(00)81515-9 contributor: fullname: Zhang – volume: 405 start-page: 85 year: 2000 ident: bib10 article-title: A receptor for phosphatidylserine-specific clearance of apoptotic cells publication-title: Nature doi: 10.1038/35011084 contributor: fullname: Fadok – volume: 420 start-page: 61 year: 2012 ident: bib30 article-title: Histone demethylase JMJD5 is essential for embryonic development publication-title: Biochemical and Biophysical Research Communications doi: 10.1016/j.bbrc.2012.02.115 contributor: fullname: Oh – volume: 92 start-page: 451 year: 1998 ident: bib44 article-title: A novel CDK9-associated C-type cyclin interacts directly with HIV-1 tat and mediates its high-affinity, loop-specific binding to TAR RNA publication-title: Cell doi: 10.1016/S0092-8674(00)80939-3 contributor: fullname: Wei – volume: 27 start-page: 262 year: 2007 ident: bib17 article-title: Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7sk capping enzyme publication-title: Molecular Cell doi: 10.1016/j.molcel.2007.06.027 contributor: fullname: Jeronimo – volume: 8 year: 2018 ident: bib26 article-title: Specific recognition of arginine methylated histone tails by JMJD5 and JMJD7 publication-title: Scientific Reports doi: 10.1038/s41598-018-21432-8 contributor: fullname: Liu – volume: 9 year: 2019 ident: bib34 article-title: De novo MEPCE nonsense variant associated with a neurodevelopmental disorder causes disintegration of 7sk snRNP and enhanced RNA polymerase II activation publication-title: Scientific Reports doi: 10.1038/s41598-019-49032-0 contributor: fullname: Schneeberger – volume: 386 start-page: 569 year: 1997 ident: bib32 article-title: Transcriptional activation by recruitment publication-title: Nature doi: 10.1038/386569a0 contributor: fullname: Ptashne – volume: 104 start-page: 10818 year: 2007 ident: bib5 article-title: Structural basis of the recognition of a methylated histone tail by JMJD2A publication-title: PNAS doi: 10.1073/pnas.0704525104 contributor: fullname: Chen – volume: 139 start-page: 749 year: 2012 ident: bib14 article-title: Jmjd5, an H3K36me2 histone demethylase, modulates embryonic cell proliferation through the regulation of Cdkn1a expression publication-title: Development doi: 10.1242/dev.074138 contributor: fullname: Ishimura – volume: 10 start-page: 339 year: 2013 ident: bib45 article-title: A Y2H-seq approach defines the human protein methyltransferase interactome publication-title: Nature Methods doi: 10.1038/nmeth.2397 contributor: fullname: Weimann – volume: 3 start-page: 92 year: 2012 ident: bib31 article-title: 7sk snRNA: a noncoding RNA that plays a major role in regulating eukaryotic transcription publication-title: Wiley Interdisciplinary Reviews: RNA doi: 10.1002/wrna.106 contributor: fullname: Peterlin – volume: 125 start-page: 467 year: 2006 ident: bib46 article-title: Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases publication-title: Cell doi: 10.1016/j.cell.2006.03.028 contributor: fullname: Whetstine – volume: 302 start-page: 1560 year: 2003 ident: bib23 article-title: Phosphatidylserine receptor is required for clearance of apoptotic cells publication-title: Science doi: 10.1126/science.1087621 contributor: fullname: Li – volume: 3 year: 2014 ident: bib35 article-title: AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter publication-title: eLife doi: 10.7554/eLife.02375 contributor: fullname: Schulze-Gahmen – volume: 517 start-page: 219 year: 2015 ident: bib29 article-title: EFF-1-mediated regenerative axonal fusion requires components of the apoptotic pathway publication-title: Nature doi: 10.1038/nature14102 contributor: fullname: Neumann – volume: 7 year: 2017 ident: bib19 article-title: Structural mechanism of the oxygenase JMJD6 recognition by the extraterminal (ET) Domain of BRD4 publication-title: Scientific Reports doi: 10.1038/s41598-017-16588-8 contributor: fullname: Konuma – volume: 293 start-page: 154 year: 2004 ident: bib9 article-title: Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals publication-title: Experimental Cell Research doi: 10.1016/j.yexcr.2003.09.023 contributor: fullname: Cui – volume: 33 start-page: 960 year: 2019 ident: bib8 article-title: Promoter-proximal pausing of RNA polymerase II: a nexus of gene regulation publication-title: Genes & Development doi: 10.1101/gad.325142.119 contributor: fullname: Core – volume: 19 start-page: 523 year: 2005 ident: bib16 article-title: The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription publication-title: Molecular Cell doi: 10.1016/j.molcel.2005.06.027 contributor: fullname: Jang – volume: 24 start-page: 248 year: 2017 ident: bib22 article-title: Catching Sirtuin-2 intermediates one structure at the time publication-title: Cell Chemical Biology doi: 10.1016/j.chembiol.2017.03.004 contributor: fullname: Lee – volume: 113 start-page: 1663 year: 2012 ident: bib12 article-title: The hydroxylation activity of Jmjd6 is required for its homo-oligomerization publication-title: Journal of Cellular Biochemistry doi: 10.1002/jcb.24035 contributor: fullname: Han – volume: 352 start-page: 104 year: 2011 ident: bib38 article-title: The Bin3 RNA methyltransferase is required for repression of caudal translation in the Drosophila embryo publication-title: Developmental Biology doi: 10.1016/j.ydbio.2011.01.017 contributor: fullname: Singh – volume: 18 start-page: 2131 year: 2017 ident: bib37 article-title: JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging stress publication-title: EMBO Reports doi: 10.15252/embr.201743892 contributor: fullname: Shen – volume: 42 start-page: 7577 year: 2014 ident: bib15 article-title: Brd4 activates P-TEFb for RNA polymerase II CTD phosphorylation publication-title: Nucleic Acids Research doi: 10.1093/nar/gku449 contributor: fullname: Itzen – volume: 38 start-page: 360 year: 2010 ident: bib48 article-title: A capping-independent function of MePCE in stabilizing 7sk snRNA and facilitating the assembly of 7sk snRNP publication-title: Nucleic Acids Research doi: 10.1093/nar/gkp977 contributor: fullname: Xue – volume: 81 start-page: 119 year: 2012 ident: bib53 article-title: RNA polymerase II elongation control publication-title: Annual Review of Biochemistry doi: 10.1146/annurev-biochem-052610-095910 contributor: fullname: Zhou – volume: 125 start-page: 691 year: 2006 ident: bib4 article-title: Structural insights into histone demethylation by JMJD2 family members publication-title: Cell doi: 10.1016/j.cell.2006.04.024 contributor: fullname: Chen – volume: 16 start-page: 167 year: 2015 ident: bib18 article-title: Getting up to speed with transcription elongation by RNA polymerase II publication-title: Nature Reviews Molecular Cell Biology doi: 10.1038/nrm3953 contributor: fullname: Jonkers – volume: 22 start-page: 1374 year: 2018 ident: bib36 article-title: Crosstalk between the RNA methylation and Histone-Binding activities of MePCE regulates P-TEFb activation on chromatin publication-title: Cell Reports doi: 10.1016/j.celrep.2018.01.028 contributor: fullname: Shelton – volume: 77 start-page: 114 year: 2009 ident: bib21 article-title: Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8 publication-title: Proteins: Structure, Function, and Bioinformatics doi: 10.1002/prot.22570 contributor: fullname: Krieger – volume: 465 start-page: 747 year: 2010 ident: bib39 article-title: Crystal structure of HIV-1 tat complexed with human P-TEFb publication-title: Nature doi: 10.1038/nature09131 contributor: fullname: Tahirov – volume: 7 year: 2017 ident: bib40 article-title: Bifunctional enzyme JMJD6 contributes to multiple disease pathogenesis: new twist on the old story publication-title: Biomolecules doi: 10.3390/biom7020041 contributor: fullname: Vangimalla – volume: 19 start-page: 535 year: 2005 ident: bib49 article-title: Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4 publication-title: Molecular Cell doi: 10.1016/j.molcel.2005.06.029 contributor: fullname: Yang – volume: 5 year: 2010 ident: bib11 article-title: Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation publication-title: PLOS ONE doi: 10.1371/journal.pone.0013769 contributor: fullname: Hahn – volume: 6 year: 2015 ident: bib51 article-title: A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells publication-title: Nature Communications doi: 10.1038/ncomms6717 contributor: fullname: Yang – volume: 114 start-page: E7717 year: 2017 ident: bib25 article-title: Clipping of arginine-methylated histone tails by JMJD5 and JMJD7 publication-title: PNAS doi: 10.1073/pnas.1706831114 contributor: fullname: Liu – volume: 44 start-page: 7527 year: 2016 ident: bib2 article-title: Cracking the control of RNA polymerase II elongation by 7sk snRNP and P-TEFb publication-title: Nucleic Acids Research doi: 10.1093/nar/gkw585 contributor: fullname: C Quaresma – volume: 327 start-page: 335 year: 2010 ident: bib28 article-title: Global analysis of short RNAs reveals widespread promoter-proximal stalling and arrest of pol II in Drosophila publication-title: Science doi: 10.1126/science.1181421 contributor: fullname: Nechaev – volume: 325 start-page: 90 year: 2009 ident: bib42 article-title: Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing publication-title: Science doi: 10.1126/science.1175865 contributor: fullname: Webby – volume: 282 start-page: 13141 year: 2007 ident: bib47 article-title: The double bromodomain-containing chromatin adaptor Brd4 and transcriptional regulation publication-title: Journal of Biological Chemistry doi: 10.1074/jbc.R700001200 contributor: fullname: Wu – volume: 318 start-page: 444 year: 2007 ident: bib3 article-title: JMJD6 is a histone arginine demethylase publication-title: Science doi: 10.1126/science.1145801 contributor: fullname: Chang – volume: 53 start-page: 819 year: 2014 ident: bib43 article-title: Nucleosomes are context-specific, H2A.Z-modulated barriers to RNA polymerase publication-title: Molecular Cell doi: 10.1016/j.molcel.2014.02.014 contributor: fullname: Weber – volume: 322 start-page: 1845 year: 2008 ident: bib7 article-title: Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters publication-title: Science doi: 10.1126/science.1162228 contributor: fullname: Core – volume: 107 start-page: 14568 year: 2010 ident: bib13 article-title: Interaction of JMJD6 with single-stranded RNA publication-title: PNAS doi: 10.1073/pnas.1008832107 contributor: fullname: Hong – volume: 3 year: 2004 ident: bib1 article-title: The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal publication-title: Journal of Biology doi: 10.1186/jbiol10 contributor: fullname: Böse – volume: 155 start-page: 1581 year: 2013 ident: bib24 article-title: Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release publication-title: Cell doi: 10.1016/j.cell.2013.10.056 contributor: fullname: Liu – volume: 369 start-page: 151 year: 1994 ident: bib20 article-title: Production of soluble MHC class II proteins with covalently bound single peptides publication-title: Nature doi: 10.1038/369151a0 contributor: fullname: Kozono – volume: 25 start-page: 742 year: 2011 ident: bib27 article-title: Regulating RNA polymerase pausing and transcription elongation in embryonic stem cells publication-title: Genes & Development doi: 10.1101/gad.2005511 contributor: fullname: Min – volume: 31 start-page: 2641 year: 2011 ident: bib33 article-title: The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3 publication-title: Molecular and Cellular Biology doi: 10.1128/MCB.01341-10 contributor: fullname: Rahman |
SSID | ssj0000748819 |
Score | 2.402386 |
Snippet | More than 30% of genes in higher eukaryotes are regulated by promoter-proximal pausing of RNA polymerase II (Pol II). Phosphorylation of Pol II CTD by positive... |
SourceID | doaj pubmedcentral proquest gale crossref pubmed |
SourceType | Open Website Open Access Repository Aggregation Database Index Database |
SubjectTerms | 7SK snRNP Analysis Animal models Animals Arginine Binding Sites Biochemistry and Chemical Biology Blotting, Western CDK9 Crystal structure Deoxyribonucleic acid DNA DNA methylation DNA-directed RNA polymerase Enzymes Gene Knockout Techniques Genes House mouse JMJD6 Mass Spectrometry MePCE Messenger RNA Methyltransferases - metabolism Mice Novels P-TEFb Phosphorylation Positive Transcriptional Elongation Factor B - metabolism Proteases Protein Structure, Tertiary Proteins Proteolysis Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Ribonucleoproteins (small nuclear) RNA RNA polymerase RNA polymerase II RNA Polymerase II - metabolism Transcription (Genetics) Transcription elongation factor b |
SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQT1wQiFegIIMqAYfQPBw7Ppayq7JiUQWt1Jvl2JPtqihB3Wwl_j0zTnaViAMXrvHk9Y3tbyaafMPYUZJA7TWoWIJWsQCAmMLqWBclEqBzqnT0QX_5TZ5disVVcTVq9UU1Yb08cA_ccY1ZMSBJgoJaOOnxnj53pRYuk0i9vdh2WoySqbAHK5yYqe5_yFNImcfwdV3DxyLXVO88oqCg1P_3fjwipGmx5Ih95g_ZgyFs5Cf94z5i96B5zFaL5eKz5HjA3sGGL-H8dMa7llMfFCQn3hdk3QHviJB22wOHn22zCg7hfbcdXvH35_HFbF594OuGX4fSDw7bG3v7u8VQ9Am7nM8uTs_ioXFC7GRadnFtq9Rrj8mKA6edLHJcqkqmLhXWqirJfVYmus5EhWhqW2LKlMgSIyeweepymT9lB03bwHPGVeG9RDdnqhIit65MvMhFXda-dt4nELGjHZbmV6-PYTCvIMhNgNwEyCP2iXDem5CodTiArjaDq82_XB2xt-QlQ7IVDdXFrOx2szFffnw3JzKVuiBpooi9G4zqFtF1dvjNAF-HlK4mlocTS1xXbjq8mwxmWNcbgwGOIL2fVEfszX6YzqRatQbaLdkUgvRPC7zEs37u7N87J51kDMkjpiazagLMdKRZXwfVb0XBoyhe_A8kX7L7GX03CI1tDtlBd7uFVxhcddXrsI7-ALCpI-g priority: 102 providerName: Directory of Open Access Journals – databaseName: ProQuest Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9NAEF6VcuGCQLxcClpQJeBg4sd6HydUSqIQEVRBK_VmrXfHaQSyS-JU4t8zYzshFhJX79qy57Hz7Xj2G8ZOoghKb0CFEowKBQCEBKtDk2kMgM4p7SihP_8qp5didpVdHbDp9iwMlVVu18R2ofa1oxz5CEOLIKaV2IxsQVkA14w-3PwKqX8U_Wftm2ncYXfjBGEFWra6UrtsCwZKjbd2B_QUhtARfFmW8D5LDdU_74Wklrn_3_V5L0ANiyf3otHkAbvfw0h-2un9ITuA6hFbzOazT5LjBXsLaz6H87Mxb2pOfVEwWPGuQOsWeEMBartccPhZV4tWQbzrvsML_vY8vBhPind8WfHrthSEw-aHXf2uEZo-ZpeT8cXZNOwbKYROxroJS1vE3njcvDhwxsksRddVMnaxsFYVUeoTHZkyEQVq1FiNW6hIakRSYNPYpTJ9wg6ruoJnjKvMe4lqT1QhRGqdjrxIRalLXzrvIwjYyVaW-U3Hl5HjPoNEnrciz1uRB-wjyXk3hUiu2wv1apH3PpOXsdGA-AgUlMJJjy_nU6eNcIlE1CUD9pq0lBONRUV1Mgu7Wa_zz9-_5acyliYjqqKAveknlTVZje2PHeDnEPPVYObxYCb6mRsOb40h7_18nf-1yoC92g3TnVS7VkG9oTmZID7UDB_xtLOd3XenxJuMED1gamBVA8EMR6rldcsCrghMiuzo_6_1nN1LKEPQtrA5ZofNagMvEEY1xcvWQ_4AFRsefA priority: 102 providerName: ProQuest – databaseName: Scholars Portal Journals: Open Access dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwdV1Lb9QwELaqIqFeEIhXSkEGVQIOWZLYseMTKmVXZcWiCrpSb1ZiT7YrqgT2UdF_z0weVcPjGk-seDzj-caafMPYYRRB6Q3oUIHRoQSAkGB1aNIMA6BzOnN0oT_7ok7mcnqenu-wvhlnp8D1P1M76ic1X12Ofv28fo8Oj_h1pDEavoPPyxJGqTACc_c7iRSSTH3W4fzmSNZop7Fp_8_78509dlcQfa0x8SA4NRz-f5_Ut0LVsIzyVlya3Gf3OkDJj1oLeMB2oHrIFtPZ9KPi-CC_gjWfwenxmG9qTh1SMGzxtlTrCviGQlV_cHC4rKtFs1W87cPDC_7mNDwbT4q3fFnxi6YohMP2e766rhGkPmLzyfjs-CTsWiqETsXZJizzIvbGYxrjwBmnUoFOrFXsYpnnuoiET7LIlIkscG9NnmEyFakMMRXkInZCicdst6oreMq4Tr1XaACJLqQUucsij5ovs9KXzvsIAnbY69L-aJkzLGYcpH3baN822g_YB9LzjQjRXTcP6tXCdt5jy9hkgEgJNJTSKY8f54XLjHSJQvylAvaKdskSoUVFFTOLfLte20_fvtojFSuTEmlRwF53QmWN2nV59wMCLoc4sAaSBwNJ9Dg3HO6NwfYGaxH6SGICik3AXt4M05tUxVZBvSWZVBIzaopTPGlt52bdvQkGTA-saqCY4Ui1vGj4wDXBSpnu_3fOZ2wvoWuCpo_NAdvdrLbwHLHUpnjR-Mlvv5EdFA priority: 102 providerName: Scholars Portal |
Title | JMJD6 cleaves MePCE to release positive transcription elongation factor b (P-TEFb) in higher eukaryotes |
URI | https://www.ncbi.nlm.nih.gov/pubmed/32048991 https://www.proquest.com/docview/2384741819/abstract/ https://search.proquest.com/docview/2354175356 https://pubmed.ncbi.nlm.nih.gov/PMC7064345 https://doaj.org/article/f198e846e7ef4c6dbecd3c894c262736 |
Volume | 9 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV07b9swECaSdOlStOhLaWqwRYC2g2LJpPgYE9dGatSBkSaAN0EiT47RRAr8CNB_3yMlGRa6ddFAHgXyHrwjcfyOkNMogsJqkKEALUMOAKELq0OdKHSAxkhl3IX-9Epc3vLJPJkfkKR9C-OT9k2-PCvvH87K5Z3PrXx8MP02T6w_mw6l86M86R-SQ8nY3hHdb78SdTLW9Vs8id6yDz-XBZwlTDNX9405qFqt444j8nj9_-7Ke26pmzK554PGL8mLJnik5_UkX5EDKF-TxWQ6-S4oNmRPsKZTmA1HdFNRVw0FXRSt07KegG6cW2o3CQr3VbnwYqF1zR2a06-z8GY0zr_RZUnvfAIIhe3vbPWnwoD0Dbkdj26Gl2FTPiE0IlabsMjy2GqLRxYDRhuRMDRYKWIT8yyTecTsQEW6GPAc5agzhQenSCiMnyBjsWGCvSVHZVXCe0JlYq1AYQ9kzjnLjIosCqBQhS2MtREE5LTlZfpYo2SkeLpw3E8991PP_YBcOD7vSBy0tW-oVou0EXBaxFoBRkUgoeBGWJycZUZpbgYCYy0RkM9OSqkDryhddswi267X6Y9f1-m5iIVOHEBRQL40REWF3DVZ89gAl-PwrjqUJx1KtC7T7W6VIW2se51imMMd6k-sA_Jp1-1Guoy1Eqqto0m4Q0FN8Bfvat3ZrbtVwYDIjlZ1GNPtQVPw2N-N6h__98gP5PnAXRn4mjYn5Giz2sJHjKs2eQ-taS575NnF6Gp23fO3E_idctXzFvYXu5Qn_w |
link.rule.ids | 230,315,733,786,790,870,891,2115,12083,21416,24346,27957,27958,31754,31755,33779,33780,43345,43840,53827,53829,74102,74659 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELege4AXBOIrY4BBk4CHsKRx7PgJbaNVV9qqGp20NyuxL10FSkY_JvHfc5ekpRESr_E5Su58_p0vl98xdhwEkDsNypeglS8AwKew2tdxggBorUosJfTHEzm4EsPr-LpJuK2assrtnlht1K60lCM_QWgRxLQS6i-3v3zqGkVfV5sWGvfZgcDxoMMOznqT6eUuy4IAmeCU-sc8hdB5AqNFDp_jSFPd8x4UVYz9_-7Le8DULprcQ6H-Y_aoCR_5aW3vJ-weFE_ZfDgefpUcL6R3sOJjmJ73-Lrk1A8FQYrXhVl3wNcETNttgsPPsphXhuF11x2e8Y9Tf9brZ5_4ouA3VQkIh82PdPm7xJD0Gbvq92bnA79poOBbGSZrP0-z0GmHhxYLVlsZR-iySoY2FGmqsiBy3STQeVdkaEmdJnh0CmSCERSkUWgjGT1nnaIs4CXjKnZOorm7KhMiSm0SOBGJPMldbp0LwGPHW12a25onw-D5glRuKpWbSuUeOyM970SI3Lq6UC7npvEVk4c6AYyLQEEurHT4cC6yiRa2KzHakh57T1YyRF9RUH3MPN2sVubi-6U5laHUMVEUeexDI5SXqF2bNr8b4OsQ41VL8qglif5l28PbxWAa_16Zv6vRY-92wzSTatYKKDckEwviQY3xFi_qtbN774j4kjE095hqraqWYtojxeKmYv9WFESK-PD_j_WWPRjMxiMzuph8e8UedilLULWxOWKd9XIDrzGUWmdvGn_5A_OFHxU |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELdgSIgXBOIrY4BBk4CH0KRx7PgJja3VVtapgk3qm5XY564CJaMfk_jvuUvS0giJ1_gcJffh-9m5_I6xwygC7zSoUIJWoQCAkGB1qNMME6C1KrN0oD--kKdXYjRNp23907Itq9ysifVC7SpLZ-Q9TC2CmFZi3fNtWcTkZPj55ldIHaToS2vbTuMuu4dyEXUzUFO1PW_BVJnh5OYXPYVJtAfncw-f0kRTBfROUqq5-_9doXdSVLd8cicfDR-xhy2Q5EeN5R-zO1A-YbPReHQiOV7Ib2HJxzA5HvBVxakzCqYr3pRo3QJfUYraLBgcflblrDYRb_rv8IJ_mISXg2Hxkc9Lfl0Xg3BY_8gXvysEp0_Z1XBweXwatq0UQivjbBX6vIiddrh9sWC1lWmCwatkbGOR56qIEtfPIu37okCb6jzDTVQkM8RSkCexTWTyjO2VVQkvGFepcxIN31eFEElus8iJRPjMO2-diyBghxtdmpuGMcPgToNUbmqVm1rlAftCet6KEM11faFazEwbNcbHOgNESKDACysdPpxLbKaF7UvEXTJg78hKhogsSnKJWb5eLs3Z92_mSMZSp0RWFLD3rZCvULs2b388wNch7quO5EFHEiPNdoc3zmDaSF-av34ZsLfbYZpJ1WslVGuSSQUxoqZ4i-eN72zfOyHmZATpAVMdr-oopjtSzq9rHnBFcFKk-_9_rDfsPgaKOT-7-PqSPejTcUHdz-aA7a0Wa3iFmGpVvK6D5Q9x9yHb |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=JMJD6+cleaves+MePCE+to+release+positive+transcription+elongation+factor+b+%28P-TEFb%29+in+higher+eukaryotes&rft.jtitle=eLife&rft.au=Lee%2C+Schuyler&rft.au=Liu%2C+Haolin&rft.au=Hill%2C+Ryan&rft.au=Chen%2C+Chunjing&rft.date=2020-02-12&rft.eissn=2050-084X&rft.volume=9&rft_id=info:doi/10.7554%2FeLife.53930&rft_id=info%3Apmid%2F32048991&rft.externalDocID=32048991 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2050-084X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2050-084X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2050-084X&client=summon |