MutL traps MutS at a DNA mismatch
DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containi...
Saved in:
| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 112; no. 35; pp. 10914 - 10919 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
01.09.2015
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL’s endonuclease activity by β-clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS–MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine thatThermus aquaticusMutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with β-clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. |
|---|---|
| AbstractList | DNA mismatch repair is the process by which errors generated during DNA replication are corrected. Mutations in the proteins that initiate mismatch repair, MutS and MutL, are associated with greater than 80% of hereditary nonpolyposis colorectal cancer (HNPCC) and many sporadic cancers. The assembly of MutS and MutL at a mismatch is an essential step for initiating repair; however, the nature of these interactions is poorly understood. Here, we have discovered that MutL fundamentally changes the properties of mismatch-bound MutS by preventing it from sliding away from the mismatch, which it normally does when isolated. This finding suggests a mechanism for localizing the activity of repair proteins near the mismatch.
DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL’s endonuclease activity by β-clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS–MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine that
Thermus aquaticus
MutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with β-clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor ( beta -clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL's endonuclease activity by beta -clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS-MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine that Thermus aquaticus MutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with beta -clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL's endonuclease activity by β-clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS-MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine that Thermus aquaticus MutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with β-clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL’s endonuclease activity by β-clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS–MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine thatThermus aquaticusMutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with β-clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. Significance DNA mismatch repair is the process by which errors generated during DNA replication are corrected. Mutations in the proteins that initiate mismatch repair, MutS and MutL, are associated with greater than 80% of hereditary nonpolyposis colorectal cancer (HNPCC) and many sporadic cancers. The assembly of MutS and MutL at a mismatch is an essential step for initiating repair; however, the nature of these interactions is poorly understood. Here, we have discovered that MutL fundamentally changes the properties of mismatch-bound MutS by preventing it from sliding away from the mismatch, which it normally does when isolated. This finding suggests a mechanism for localizing the activity of repair proteins near the mismatch. DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA mismatch, MutS, MutL, and the replication processivity factor (β-clamp or PCNA) activate the latent MutL endonuclease to nick the error-containing daughter strand. This nick provides an entry point for downstream repair proteins. Despite the well-established significance of strand-specific nicking in MMR, the mechanism(s) by which MutS and MutL assemble on mismatch DNA to allow the subsequent activation of MutL’s endonuclease activity by β-clamp/PCNA remains elusive. In both prokaryotes and eukaryotes, MutS homologs undergo conformational changes to a mobile clamp state that can move away from the mismatch. However, the function of this MutS mobile clamp is unknown. Furthermore, whether the interaction with MutL leads to a mobile MutS–MutL complex or a mismatch-localized complex is hotly debated. We used single molecule FRET to determine that Thermus aquaticus MutL traps MutS at a DNA mismatch after recognition but before its conversion to a sliding clamp. Rather than a clamp, a conformationally dynamic protein assembly typically containing more MutL than MutS is formed at the mismatch. This complex provides a local marker where interaction with β-clamp/PCNA could distinguish parent/daughter strand identity. Our finding that MutL fundamentally changes MutS actions following mismatch detection reframes current thinking on MMR signaling processes critical for genomic stability. |
| Author | Zhang, Xingdong Qiu, Ruoyi Wilkins, Hunter Erie, Dorothy A. Sacho, Elizabeth J. Weninger, Keith R. Hingorani, Manju M. Sakato, Miho Modrich, Paul |
| Author_xml | – sequence: 1 givenname: Ruoyi surname: Qiu fullname: Qiu, Ruoyi organization: Department of Physics, North Carolina State University, Raleigh, NC 27695 – sequence: 2 givenname: Miho surname: Sakato fullname: Sakato, Miho organization: Molecular Biology and Biochemistry Department, Wesleyan University, Middletown, CT 06459 – sequence: 3 givenname: Elizabeth J. surname: Sacho fullname: Sacho, Elizabeth J. organization: Department of Physics, North Carolina State University, Raleigh, NC 27695 – sequence: 4 givenname: Hunter surname: Wilkins fullname: Wilkins, Hunter organization: Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 – sequence: 5 givenname: Xingdong surname: Zhang fullname: Zhang, Xingdong organization: Department of Biochemistry, Duke University Medical Center, Durham, NC 27710 – sequence: 6 givenname: Paul surname: Modrich fullname: Modrich, Paul organization: Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710 – sequence: 7 givenname: Manju M. surname: Hingorani fullname: Hingorani, Manju M. organization: Molecular Biology and Biochemistry Department, Wesleyan University, Middletown, CT 06459 – sequence: 8 givenname: Dorothy A. surname: Erie fullname: Erie, Dorothy A. organization: Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 – sequence: 9 givenname: Keith R. surname: Weninger fullname: Weninger, Keith R. organization: Department of Physics, North Carolina State University, Raleigh, NC 27695 |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26283381$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNkbtPwzAQhy0EgvKYmUBBLCxp7_yMFyTEWyowALPluA60apMSJ0j89zhqKY-JyZb83c93922T9bIqPSH7CH0ExQbz0oY-ChBSCES6RnoIGlPJNayTHgBVacYp3yLbIUwAQIsMNskWlTRjLMMeObprm2HS1HYeknh9TGyT2OTi_iyZjcPMNu51l2wUdhr83vLcIc9Xl0_nN-nw4fr2_GyYOiFVk3rwwArQPM8Yx1wopy0W1kk9AqsUL6RWuSqYk2ApSJlLhTl1oFzh8xFVbIecLnLnbT7zI-fL2NXUzOvxzNYfprJj8_ulHL-al-rdcCEzmtEYcLIMqKu31ofGxBGcn05t6as2GFRUSZUpUP9AQTNNNWJEj_-gk6qty7iJSGHcNpOy-3uwoFxdhVD7YtU3gulMmc6U-TYVKw5_jrviv9REIFkCXeUqDqlhwnSWeUQOFsgkNFX9I4JLHgH2CWJWoeI |
| CitedBy_id | crossref_primary_10_1134_S1068162021020205 crossref_primary_10_1021_acs_chemrestox_8b00179 crossref_primary_10_1093_nar_gkad418 crossref_primary_10_1038_s41467_022_33479_3 crossref_primary_10_1016_j_dnarep_2015_11_012 crossref_primary_10_3390_cells10061535 crossref_primary_10_1016_j_jmb_2018_05_039 crossref_primary_10_1093_nar_gky1168 crossref_primary_10_1016_j_dnarep_2018_06_002 crossref_primary_10_1093_nar_gkz834 crossref_primary_10_1093_nar_gky865 crossref_primary_10_3390_cells11030521 crossref_primary_10_1073_pnas_1918517117 crossref_primary_10_7554_eLife_15155 crossref_primary_10_1038_nature20562 crossref_primary_10_1073_pnas_1918519117 crossref_primary_10_1128_MMBR_00008_20 crossref_primary_10_1016_j_dnarep_2015_11_014 crossref_primary_10_1016_j_dnarep_2015_11_013 crossref_primary_10_1128_mSphere_00433_21 crossref_primary_10_1038_s41467_024_48784_2 crossref_primary_10_1016_j_dnarep_2015_11_017 crossref_primary_10_1002_em_22087 crossref_primary_10_1021_acsinfecdis_9b00220 crossref_primary_10_1002_bip_22843 crossref_primary_10_1002_path_4948 crossref_primary_10_1038_s41594_021_00577_7 crossref_primary_10_1016_j_lfs_2022_120852 crossref_primary_10_1038_s41422_021_00468_y crossref_primary_10_1093_nar_gkw411 crossref_primary_10_1093_nar_gkad096 crossref_primary_10_1016_j_jbc_2022_102505 crossref_primary_10_1007_s42764_022_00094_x crossref_primary_10_1038_s41467_019_08769_y crossref_primary_10_1146_annurev_biophys_070816_034106 crossref_primary_10_1016_j_semcdb_2017_06_028 crossref_primary_10_1021_acs_jpcb_6b11976 crossref_primary_10_1016_j_dnarep_2021_103161 crossref_primary_10_1038_s41594_021_00713_3 crossref_primary_10_1073_pnas_1523748113 |
| Cites_doi | 10.1016/S1046-2023(02)00308-0 10.1016/j.bpj.2010.04.049 10.1016/j.canlet.2006.08.008 10.1093/nar/gkr1298 10.1002/humu.22168 10.1074/jbc.275.3.2080 10.1074/jbc.273.15.9202 10.1074/jbc.M114.552190 10.1016/j.jmb.2006.11.092 10.1016/S0021-9258(19)85043-3 10.1016/j.molcel.2010.06.027 10.1146/annurev.bi.56.070187.002251 10.1016/j.cell.2006.05.039 10.1038/nsmb.2009 10.1016/j.mad.2008.02.012 10.1038/emboj.2012.95 10.1016/j.dnarep.2010.10.003 10.1074/jbc.273.16.9837 10.1021/bi049010t 10.1073/pnas.1308595110 10.7554/eLife.06744.021 10.1007/s10689-013-9635-x 10.1073/pnas.1311325110 10.1016/S1097-2765(03)00219-3 10.1021/bi901871u 10.1074/jbc.M109.054528 10.1016/j.dnarep.2014.03.007 10.1021/cr0404794 10.1016/j.cell.2011.10.025 10.1074/jbc.M202282200 10.1146/annurev.biochem.74.082803.133243 10.1074/jbc.M407545200 10.1016/S1097-2765(00)80316-0 10.1073/pnas.2433654100 10.1074/jbc.M103148200 10.1016/j.jmb.2013.08.011 10.1073/pnas.1211364109 10.1021/bi401429b 10.1074/jbc.M707617200 10.1126/science.1084398 10.1073/pnas.1010662107 |
| ContentType | Journal Article |
| Copyright | Volumes 1–89 and 106–112, copyright as a collective work only; author(s) retains copyright to individual articles Copyright National Academy of Sciences Sep 1, 2015 |
| Copyright_xml | – notice: Volumes 1–89 and 106–112, copyright as a collective work only; author(s) retains copyright to individual articles – notice: Copyright National Academy of Sciences Sep 1, 2015 |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QG 7QL 7QP 7QR 7SN 7SS 7T5 7TK 7TM 7TO 7U9 8FD C1K FR3 H94 M7N P64 RC3 7X8 5PM |
| DOI | 10.1073/pnas.1505655112 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Ecology Abstracts Entomology Abstracts (Full archive) Immunology Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Oncogenes and Growth Factors Abstracts Virology and AIDS Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database AIDS and Cancer Research Abstracts Algology Mycology and Protozoology Abstracts (Microbiology C) Biotechnology and BioEngineering Abstracts Genetics Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Virology and AIDS Abstracts Oncogenes and Growth Factors Abstracts Technology Research Database Nucleic Acids Abstracts Ecology Abstracts Neurosciences Abstracts Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management Entomology Abstracts Genetics Abstracts Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts Chemoreception Abstracts Immunology Abstracts Engineering Research Database Calcium & Calcified Tissue Abstracts MEDLINE - Academic |
| DatabaseTitleList | Nucleic Acids Abstracts MEDLINE Virology and AIDS Abstracts MEDLINE - Academic CrossRef |
| Database_xml | – sequence: 1 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: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Sciences (General) |
| DocumentTitleAlternate | MutL traps MutS at a DNA mismatch |
| EISSN | 1091-6490 |
| EndPage | 10919 |
| ExternalDocumentID | 3803900611 10_1073_pnas_1505655112 26283381 112_35_10914 26464091 |
| Genre | Research Support, U.S. Gov't, Non-P.H.S Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural Feature |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: GM045190 – fundername: NIGMS NIH HHS grantid: GM080294 – fundername: Howard Hughes Medical Institute – fundername: NIGMS NIH HHS grantid: GM109832 – fundername: NIGMS NIH HHS grantid: R01 GM109832 – fundername: NIGMS NIH HHS grantid: R01 GM080294 – fundername: NIGMS NIH HHS grantid: R01 GM079480 – fundername: NIGMS NIH HHS grantid: GM079480 – fundername: NIGMS NIH HHS grantid: R01 GM045190 – fundername: HHS | National Institutes of Health (NIH) grantid: GM079480 – fundername: Howard Hughes Medical Institute (HHMI) grantid: none – fundername: American Cancer Society (ACS) grantid: RSG-10-048 – fundername: National Science Foundation (NSF) grantid: MCB 1022203 – fundername: HHS | National Institutes of Health (NIH) grantid: GM080294 – fundername: HHS | National Institutes of Health (NIH) grantid: GM045190 |
| GroupedDBID | --- -DZ -~X .55 0R~ 123 29P 2AX 2FS 2WC 4.4 53G 5RE 5VS 79B 85S AACGO AAFWJ AANCE ABBHK ABOCM ABPLY ABPPZ ABTLG ABXSQ ABZEH ACGOD ACIWK ACNCT ACPRK ADULT ADZLD AENEX AEUPB AEXZC AFFNX AFOSN AFRAH ALMA_UNASSIGNED_HOLDINGS AQVQM ASUFR BKOMP CS3 D0L DCCCD DIK DNJUQ DOOOF DU5 DWIUU E3Z EBS EJD F5P FRP GX1 HH5 HYE JAAYA JBMMH JENOY JHFFW JKQEH JLS JLXEF JPM JSG JSODD JST KQ8 L7B LU7 N9A N~3 O9- OK1 PNE PQQKQ R.V RHF RHI RNA RNS RPM RXW SA0 SJN TAE TN5 UKR VQA W8F WH7 WOQ WOW X7M XSW Y6R YBH YKV YSK ZA5 ZCA ~02 ~KM - 02 0R 1AW 55 AAPBV ABFLS ABPTK ADACO DZ F20 H13 KM PQEST X XHC ADACV CGR CUY CVF ECM EIF IPSME NPM .GJ 3O- 692 6TJ AAYJJ AAYXX ACKIV AS~ CITATION HGD HQ3 HTVGU MVM NEJ NHB P-O VOH WHG ZCG 7QG 7QL 7QP 7QR 7SN 7SS 7T5 7TK 7TM 7TO 7U9 8FD C1K FR3 H94 M7N P64 RC3 7X8 ADQXQ 5PM |
| ID | FETCH-LOGICAL-c567t-e0e03f094b8341b57c9a1fac69d0a774f697b7f3c60a2066b671b2c07cfebd273 |
| IEDL.DBID | RPM |
| ISSN | 0027-8424 |
| IngestDate | Tue Sep 17 21:13:15 EDT 2024 Sat Aug 17 01:46:51 EDT 2024 Fri Aug 16 05:39:50 EDT 2024 Thu Oct 10 18:35:00 EDT 2024 Fri Aug 23 01:52:09 EDT 2024 Sat Sep 28 08:04:54 EDT 2024 Wed Nov 11 00:29:36 EST 2020 Fri Feb 02 08:16:18 EST 2024 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 35 |
| Keywords | FRET MutS MutL DNA mismatch repair |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c567t-e0e03f094b8341b57c9a1fac69d0a774f697b7f3c60a2066b671b2c07cfebd273 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by John A. Tainer, Scripps Research Institute, La Jolla, CA, and accepted by the Editorial Board July 21, 2015 (received for review March 20, 2015) Author contributions: R.Q., M.M.H., D.A.E., and K.R.W. designed research; R.Q., M.S., E.J.S., H.W., and D.A.E. performed research; R.Q., M.S., H.W., X.Z., P.M., M.M.H., and K.R.W. contributed new reagents/analytic tools; R.Q., M.S., E.J.S., M.M.H., D.A.E., and K.R.W. analyzed data; and P.M., M.M.H., D.A.E., and K.R.W. wrote the paper. |
| OpenAccessLink | https://www.pnas.org/content/pnas/112/35/10914.full.pdf |
| PMID | 26283381 |
| PQID | 1711093662 |
| PQPubID | 42026 |
| PageCount | 6 |
| ParticipantIDs | proquest_miscellaneous_1709392911 crossref_primary_10_1073_pnas_1505655112 jstor_primary_26464091 pubmedcentral_primary_oai_pubmedcentral_nih_gov_4568282 pubmed_primary_26283381 pnas_primary_112_35_10914 proquest_miscellaneous_1727678707 proquest_journals_1711093662 |
| ProviderPackageCode | RNA PNE |
| PublicationCentury | 2000 |
| PublicationDate | 2015-09-01 |
| PublicationDateYYYYMMDD | 2015-09-01 |
| PublicationDate_xml | – month: 09 year: 2015 text: 2015-09-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: Washington |
| PublicationTitle | Proceedings of the National Academy of Sciences - PNAS |
| PublicationTitleAlternate | Proc Natl Acad Sci U S A |
| PublicationYear | 2015 |
| Publisher | National Academy of Sciences National Acad Sciences |
| Publisher_xml | – name: National Academy of Sciences – name: National Acad Sciences |
| References | 22118461 - Cell. 2011 Nov 23;147(5):1040-53 16873062 - Cell. 2006 Jul 28;126(2):297-308 19783657 - J Biol Chem. 2009 Nov 20;284(47):32782-91 21050827 - DNA Repair (Amst). 2011 Jan 2;10(1):87-93 17029773 - Cancer Lett. 2007 May 8;249(2):148-56 20643053 - Biophys J. 2010 Jul 21;99(2):360-6 18406444 - Mech Ageing Dev. 2008 Jul-Aug;129(7-8):391-407 15952900 - Annu Rev Biochem. 2005;74:681-710 20713735 - Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16066-71 24101514 - Proc Natl Acad Sci U S A. 2013 Oct 22;110(43):17308-13 20603082 - Mol Cell. 2010 Jul 9;39(1):145-51 23572416 - Fam Cancer. 2013 Jun;12(2):159-68 12606223 - Methods. 2003 Feb;29(2):175-87 12887908 - Mol Cell. 2003 Jul;12(1):233-46 26163658 - Elife. 2015;4:e06744 11371566 - J Biol Chem. 2001 Jul 27;276(30):28291-9 23973435 - J Mol Biol. 2013 Nov 15;425(22):4192-205 9545323 - J Biol Chem. 1998 Apr 17;273(16):9837-41 10636912 - J Biol Chem. 2000 Jan 21;275(3):2080-6 22505031 - EMBO J. 2012 May 30;31(11):2528-40 3304141 - Annu Rev Biochem. 1987;56:435-66 17951253 - J Biol Chem. 2007 Dec 21;282(51):37181-90 22241777 - Nucleic Acids Res. 2012 May;40(9):3929-38 10078208 - Mol Cell. 1999 Feb;3(2):255-61 16464007 - Chem Rev. 2006 Feb;106(2):302-23 22833534 - Hum Mutat. 2012 Dec;33(12):1617-25 11986324 - J Biol Chem. 2002 Jul 12;277(28):25545-53 23840062 - Proc Natl Acad Sci U S A. 2013 Jul 23;110(30):12277-82 20180598 - Biochemistry. 2010 Apr 13;49(14):3174-90 23012240 - Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):E3074-83 24746644 - DNA Repair (Amst). 2014 Aug;20:71-81 12791999 - Science. 2003 Jun 27;300(5628):2061-5 21278758 - Nat Struct Mol Biol. 2011 Mar;18(3):379-85 14634210 - Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14822-7 15811858 - J Biol Chem. 2005 Jun 10;280(23):22245-57 9535911 - J Biol Chem. 1998 Apr 10;273(15):9202-7 15476405 - Biochemistry. 2004 Oct 19;43(41):13115-28 2536011 - J Biol Chem. 1989 Jan 15;264(2):1000-4 24550389 - J Biol Chem. 2014 Mar 28;289(13):9352-64 24588663 - Biochemistry. 2014 Apr 1;53(12):2043-52 17207499 - J Mol Biol. 2007 Mar 2;366(4):1087-98 e_1_3_3_17_2 e_1_3_3_16_2 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_18_2 e_1_3_3_39_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_32_2 e_1_3_3_33_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_10_2 e_1_3_3_31_2 e_1_3_3_40_2 e_1_3_3_6_2 e_1_3_3_5_2 e_1_3_3_8_2 e_1_3_3_7_2 e_1_3_3_28_2 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_29_2 e_1_3_3_24_2 e_1_3_3_23_2 e_1_3_3_26_2 e_1_3_3_25_2 e_1_3_3_2_2 e_1_3_3_20_2 e_1_3_3_1_2 e_1_3_3_4_2 e_1_3_3_22_2 e_1_3_3_41_2 e_1_3_3_3_2 e_1_3_3_21_2 |
| References_xml | – ident: e_1_3_3_40_2 doi: 10.1016/S1046-2023(02)00308-0 – ident: e_1_3_3_26_2 doi: 10.1016/j.bpj.2010.04.049 – ident: e_1_3_3_13_2 doi: 10.1016/j.canlet.2006.08.008 – ident: e_1_3_3_22_2 doi: 10.1093/nar/gkr1298 – ident: e_1_3_3_2_2 doi: 10.1002/humu.22168 – ident: e_1_3_3_19_2 doi: 10.1074/jbc.275.3.2080 – ident: e_1_3_3_35_2 doi: 10.1074/jbc.273.15.9202 – ident: e_1_3_3_23_2 doi: 10.1074/jbc.M114.552190 – ident: e_1_3_3_38_2 doi: 10.1016/j.jmb.2006.11.092 – ident: e_1_3_3_3_2 doi: 10.1016/S0021-9258(19)85043-3 – ident: e_1_3_3_14_2 doi: 10.1016/j.molcel.2010.06.027 – ident: e_1_3_3_7_2 doi: 10.1146/annurev.bi.56.070187.002251 – ident: e_1_3_3_9_2 doi: 10.1016/j.cell.2006.05.039 – ident: e_1_3_3_20_2 doi: 10.1038/nsmb.2009 – ident: e_1_3_3_8_2 doi: 10.1016/j.mad.2008.02.012 – ident: e_1_3_3_21_2 doi: 10.1038/emboj.2012.95 – ident: e_1_3_3_36_2 doi: 10.1016/j.dnarep.2010.10.003 – ident: e_1_3_3_4_2 doi: 10.1074/jbc.273.16.9837 – ident: e_1_3_3_29_2 doi: 10.1021/bi049010t – ident: e_1_3_3_31_2 doi: 10.1073/pnas.1308595110 – ident: e_1_3_3_41_2 doi: 10.7554/eLife.06744.021 – ident: e_1_3_3_1_2 doi: 10.1007/s10689-013-9635-x – ident: e_1_3_3_12_2 doi: 10.1073/pnas.1311325110 – ident: e_1_3_3_24_2 doi: 10.1016/S1097-2765(03)00219-3 – ident: e_1_3_3_37_2 doi: 10.1021/bi901871u – ident: e_1_3_3_34_2 doi: 10.1074/jbc.M109.054528 – ident: e_1_3_3_5_2 doi: 10.1016/j.dnarep.2014.03.007 – ident: e_1_3_3_6_2 doi: 10.1021/cr0404794 – ident: e_1_3_3_18_2 doi: 10.1016/j.cell.2011.10.025 – ident: e_1_3_3_30_2 doi: 10.1074/jbc.M202282200 – ident: e_1_3_3_15_2 doi: 10.1146/annurev.biochem.74.082803.133243 – ident: e_1_3_3_39_2 doi: 10.1074/jbc.M407545200 – ident: e_1_3_3_17_2 doi: 10.1016/S1097-2765(00)80316-0 – ident: e_1_3_3_33_2 doi: 10.1073/pnas.2433654100 – ident: e_1_3_3_25_2 doi: 10.1074/jbc.M103148200 – ident: e_1_3_3_28_2 doi: 10.1016/j.jmb.2013.08.011 – ident: e_1_3_3_16_2 doi: 10.1073/pnas.1211364109 – ident: e_1_3_3_32_2 doi: 10.1021/bi401429b – ident: e_1_3_3_11_2 doi: 10.1074/jbc.M707617200 – ident: e_1_3_3_27_2 doi: 10.1126/science.1084398 – ident: e_1_3_3_10_2 doi: 10.1073/pnas.1010662107 |
| SSID | ssj0009580 |
| Score | 2.4443483 |
| Snippet | DNA mismatch repair (MMR) identifies and corrects errors made during replication. In all organisms except those expressing MutH, interactions between a DNA... Significance DNA mismatch repair is the process by which errors generated during DNA replication are corrected. Mutations in the proteins that initiate... DNA mismatch repair is the process by which errors generated during DNA replication are corrected. Mutations in the proteins that initiate mismatch repair,... |
| SourceID | pubmedcentral proquest crossref pubmed pnas jstor |
| SourceType | Open Access Repository Aggregation Database Index Database Publisher |
| StartPage | 10914 |
| SubjectTerms | Bacterial Proteins - genetics Base Pair Mismatch Biological Sciences DNA repair Eukaryotes Genes, Bacterial Prokaryotes Proteins Thermus - genetics Thermus aquaticus |
| Title | MutL traps MutS at a DNA mismatch |
| URI | https://www.jstor.org/stable/26464091 http://www.pnas.org/content/112/35/10914.abstract https://www.ncbi.nlm.nih.gov/pubmed/26283381 https://www.proquest.com/docview/1711093662 https://search.proquest.com/docview/1709392911 https://search.proquest.com/docview/1727678707 https://pubmed.ncbi.nlm.nih.gov/PMC4568282 |
| Volume | 112 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8QwEB50T17Et_VFBA966G7TNEn3KOoi4oqggreSpAkKbl3c7v930peuiAdvhUyGMpPk-9JMvgKcGMYkcyYOjch5iHgbh4omNsRl0AmbCqm5vzs8vhPXT8nNM39eAt7ehamK9o1-7Rdvk37x-lLVVk4nZtDWiQ3uxxcI-rhRiAfLsCwZa7fondJuWt87iXH5TeKk1fORbDAt1KxPPeZzzzO8ELBAeGUpXUClujDRq52i_W_M82cB5TdEGq3BakMlyXn9yuuwZIsNWG8m64ycNorSZ5twPJ6XtwR9TGcEHx-IKokil3fnBLOMlNW8bMHT6Orx4jps_o0QGi5kGdrIRszh3kyniEOaSzNU1CkjhnmkkNI5MZRaOmZEpLxiuxaS6thE0jirc-Qs29Ar3gu7CyRXzvjPGqnFaOXGoE-ROC0NpyKyKg3gtI1NNq0lMLLq6FqyzEco-4poANtV7Do7pFsCd5A0gKAy7frTOGPcH3_TJICDNsJZM4HQp_RSqEwI9HncNWNQ_HmGKuz73NugBdI7Sv-yiaXwi5IMYKdO2reXq5MfgFxIZ2fgpbcXW3BEVhLczQjc-3fPfVhB6sXrarUD6JUfc3uI9KbURx5c-FE1qD8BS2H1cg |
| link.rule.ids | 230,315,733,786,790,891,27955,27956,53825,53827 |
| linkProvider | National Library of Medicine |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwEB2VcoALtEBLoAVX4lAOycZ2bGePVUu1wO4KiRb1FtmOrVbQdMVmL_x6xvlqt0JIcIvkseV4xjNv4vELwDvLueLestjKUsQYb1msaeZidINeulwqI8Ld4dlcTs6zTxfiYgNEfxemKdq35iqpflwn1dVlU1u5uLajvk5s9GV2jEEfEwU2egAPcb8y0SfpA9du3t48YeiAM5b1jD6KjxaVXiY0RH0RkEagApYYYHlO1-JSW5oY-E5R_k_Y834J5Z2YdPoUvvVv05aifE9WtUnsr3tEj__8ulvwpEOp5Kht3oYNVz2D7c4PLMlhR1b9_jkczFb1lODkFkuCj1-JrokmJ_MjggaEaNhevoDz0w9nx5O4--1CbIVUdexSl3KPaZ_JMcQZoexYU6-tHJepRrTo5VgZ5bmVqQ5k8EYqaphNlfXOlAiHdmCzuqncSyCl9jZ8MckdqqG0FseUmTfKCipTp_MIDvtFLxYtu0bRnIorXoSlL25VFcFOo5RBDpGcxOSURhA1okN_ygouwsk6zSLY61VXdHsTx1SBZZVLiWMeDM24KOGoRFfuZhVkUAKRI6V_k2FKBn-nIthtreHO5FqrikCt2ckgEFi911tQ-w27d6ftV__d8y08mpzNpsX04_zza3iMCE-0RXF7sFn_XLl9RFG1edPsmd-0HxaU |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB5BkRAXaIGWQAuuxKEc8nAc29lj1XZVoLuqBJUqLpHt2GoFTSM2e-HXM86ruxXi0Fskjy3bM575HI8_A3w0jEnmTBoaUfIQ420aKprZEN2gEzYXUnN_d3g2F6cX2ZdLfrny1FebtG_0dVT9uomq66s2t7K-MfGQJxafz44w6ONGIY3r0sWP4Qmu2VQOG_WRbzfvbp-k6ISzNBtYfSSL60otIuojP_dow9MBCwyyLKdrsalLT_Scpyj_L_x5P41yJS5NX8CPYURdOsrPaNnoyPy5R_b4oCFvwvMerZLDTmQLHtnqJWz1_mBBDnrS6k-vYH-2bM4IdrBeEPz8RlRDFDmeHxI0JETF5uo1XExPvh-dhv3zC6HhQjahTWzCHG7_dI6hTnNpJoo6ZcSkTBSiRicmUkvHjEiUJ4XXQlKdmkQaZ3WJsGgbNqrbyr4BUipn_J-T3KIqSmOwTZE5LQ2nIrEqD-BgmPii7lg2ivZ0XLLCT39xp64AtlvFjHKI6ARuUmkAQSs61qdpwbg_YadZALuD-op-jWKb0rOtMiGwzf2xGCfFH5moyt4uvQxKIIKk9H8yqRTe78kAdjqLWOlcZ1kByDVbGQU8u_d6CVpAy_Lda_ztg2t-gKfnx9Pi7PP86zt4hkCPd7lxu7DR_F7aPQRTjX7fLpu_l0QZFA |
| 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=MutL+traps+MutS+at+a+DNA+mismatch&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+-+PNAS&rft.au=Qiu%2C+Ruoyi&rft.au=Sakato%2C+Miho&rft.au=Sacho%2C+Elizabeth+J.&rft.au=Wilkins%2C+Hunter&rft.date=2015-09-01&rft.issn=0027-8424&rft.eissn=1091-6490&rft.volume=112&rft.issue=35&rft.spage=10914&rft.epage=10919&rft_id=info:doi/10.1073%2Fpnas.1505655112&rft.externalDBID=n%2Fa&rft.externalDocID=10_1073_pnas_1505655112 |
| thumbnail_m | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fwww.pnas.org%2Fcontent%2F112%2F35.cover.gif |
| thumbnail_s | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fwww.pnas.org%2Fcontent%2F112%2F35.cover.gif |