Evolution of the regulatory subunits for the heteromeric acetyl-CoA carboxylase
The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues ar...
Saved in:
| Published in | Philosophical transactions of the Royal Society of London. Series B. Biological sciences Vol. 379; no. 1914; p. 20230353 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Royal Society, The
18.11.2024
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues are comprised both catalytic and additional dedicated regulatory subunits. Novel regulatory subunits, biotin lipoyl attachment domain-containing proteins (BADC) and carboxyltransferase interactors (CTI) (both three-gene families in
) represent new effectors specific to plants and certain algal species. The evolutionary history of these genes in autotrophic eukaryotes remains elusive, making it an ongoing area of research. Analyses of potential protein-protein and co-occurrence interactions, informed by gene network patterns using the STRING database, in
and
unveil intricate gene associations with ACCase, suggesting a complex interplay between FA synthesis and other cellular processes. Among both species, a higher number of co-expressed genes was identified in
, indicating a wider potential regulatory network of ACCase in plants. This review investigates the extent to which these genes arose in autotrophic eukaryotes and provides insights into their evolutionary trajectory. This article is part of the theme issue 'The evolution of plant metabolism'. |
|---|---|
| AbstractList | The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues are comprised both catalytic and additional dedicated regulatory subunits. Novel regulatory subunits, biotin lipoyl attachment domain-containing proteins (BADC) and carboxyltransferase interactors (CTI) (both three-gene families in Arabidopsis) represent new effectors specific to plants and certain algal species. The evolutionary history of these genes in autotrophic eukaryotes remains elusive, making it an ongoing area of research. Analyses of potential protein-protein and co-occurrence interactions, informed by gene network patterns using the STRING database, in Arabidopsis thaliana and Chlamydomonas reinhardtii unveil intricate gene associations with ACCase, suggesting a complex interplay between FA synthesis and other cellular processes. Among both species, a higher number of co-expressed genes was identified in Arabidopsis, indicating a wider potential regulatory network of ACCase in plants. This review investigates the extent to which these genes arose in autotrophic eukaryotes and provides insights into their evolutionary trajectory. This article is part of the theme issue 'The evolution of plant metabolism'.The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues are comprised both catalytic and additional dedicated regulatory subunits. Novel regulatory subunits, biotin lipoyl attachment domain-containing proteins (BADC) and carboxyltransferase interactors (CTI) (both three-gene families in Arabidopsis) represent new effectors specific to plants and certain algal species. The evolutionary history of these genes in autotrophic eukaryotes remains elusive, making it an ongoing area of research. Analyses of potential protein-protein and co-occurrence interactions, informed by gene network patterns using the STRING database, in Arabidopsis thaliana and Chlamydomonas reinhardtii unveil intricate gene associations with ACCase, suggesting a complex interplay between FA synthesis and other cellular processes. Among both species, a higher number of co-expressed genes was identified in Arabidopsis, indicating a wider potential regulatory network of ACCase in plants. This review investigates the extent to which these genes arose in autotrophic eukaryotes and provides insights into their evolutionary trajectory. This article is part of the theme issue 'The evolution of plant metabolism'. The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues are comprised both catalytic and additional dedicated regulatory subunits. Novel regulatory subunits, biotin lipoyl attachment domain-containing proteins (BADC) and carboxyltransferase interactors (CTI) (both three-gene families in Arabidopsis ) represent new effectors specific to plants and certain algal species. The evolutionary history of these genes in autotrophic eukaryotes remains elusive, making it an ongoing area of research. Analyses of potential protein–protein and co-occurrence interactions, informed by gene network patterns using the STRING database, in Arabidopsis thaliana and Chlamydomonas reinhardtii unveil intricate gene associations with ACCase, suggesting a complex interplay between FA synthesis and other cellular processes. Among both species, a higher number of co-expressed genes was identified in Arabidopsis , indicating a wider potential regulatory network of ACCase in plants. This review investigates the extent to which these genes arose in autotrophic eukaryotes and provides insights into their evolutionary trajectory. This article is part of the theme issue ‘The evolution of plant metabolism’. The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase). In most plants, ACCase is a multi-subunit complex orthologous to prokaryotes. However, unlike prokaryotes, the plant and algal orthologues are comprised both catalytic and additional dedicated regulatory subunits. Novel regulatory subunits, biotin lipoyl attachment domain-containing proteins (BADC) and carboxyltransferase interactors (CTI) (both three-gene families in ) represent new effectors specific to plants and certain algal species. The evolutionary history of these genes in autotrophic eukaryotes remains elusive, making it an ongoing area of research. Analyses of potential protein-protein and co-occurrence interactions, informed by gene network patterns using the STRING database, in and unveil intricate gene associations with ACCase, suggesting a complex interplay between FA synthesis and other cellular processes. Among both species, a higher number of co-expressed genes was identified in , indicating a wider potential regulatory network of ACCase in plants. This review investigates the extent to which these genes arose in autotrophic eukaryotes and provides insights into their evolutionary trajectory. This article is part of the theme issue 'The evolution of plant metabolism'. |
| Author | Conrado, Ana Caroline Rao, R S P Lemes Jorge, Gabriel Xu, Chunhui Thelen, Jay J Li-Beisson, Yonghua Xu, Dong |
| Author_xml | – sequence: 1 givenname: Ana Caroline orcidid: 0000-0002-8608-8546 surname: Conrado fullname: Conrado, Ana Caroline organization: Division of Biochemistry and Interdisciplinary Plant Grou, C.S. Bond Life Sciences Center, University of Missouri , Columbia, MO 65211, USA – sequence: 2 givenname: Gabriel surname: Lemes Jorge fullname: Lemes Jorge, Gabriel organization: Division of Biochemistry and Interdisciplinary Plant Grou, C.S. Bond Life Sciences Center, University of Missouri , Columbia, MO 65211, USA – sequence: 3 givenname: R S P surname: Rao fullname: Rao, R S P organization: Center for Bioinformatics, NITTE University Centre , Mangaluru 575018, India – sequence: 4 givenname: Chunhui surname: Xu fullname: Xu, Chunhui organization: Institute for Data Science and Informatics, C.S. Bond Life Sciences Center, University of Missouri , Columbia, MO 65211, USA – sequence: 5 givenname: Dong surname: Xu fullname: Xu, Dong organization: Department of Electrical Engineering and Computer Science, Institute for Data Science and Informatics, C.S. Bond Life Sciences Center, University of Missouri , Columbia, MO 65211, USA – sequence: 6 givenname: Yonghua surname: Li-Beisson fullname: Li-Beisson, Yonghua organization: Aix Marseille Univ, CEA, CNRS, BIAM, Institut de Biosciences et Biotechnologies Aix-Marseille,Aix Marseille Univ, CEA Cadarache , Saint Paul-Lez-Durance 13108, France – sequence: 7 givenname: Jay J surname: Thelen fullname: Thelen, Jay J organization: Division of Biochemistry and Interdisciplinary Plant Grou, C.S. Bond Life Sciences Center, University of Missouri , Columbia, MO 65211, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39343023$$D View this record in MEDLINE/PubMed https://hal.science/hal-04715523$$DView record in HAL |
| BookMark | eNo9kDtPwzAUhS1UBOWxMqKMMKRcPxLHY1UVilSJBWbLdm5oUBqDnVT035NQ6HSlc79zhu-CTFrfIiE3FGYUVPEQYmdnDBifAc_4CZlSIWnKlIQJmYLKWVoInp-Tixg_AEBlUpyRc6644ENpSl6WO9_0Xe3bxFdJt8Ek4HvfmM6HfRJ727d1F5PKh9_fBjsMfouhdolx2O2bdOHniTPB-u99YyJekdPKNBGv_-4leXtcvi5W6frl6XkxX6eOMsVTzIWrSuVKkK5Q1lopC8wAZCmtQ2osA2C5YVKUmOVUVkKVtgQnwTkmhOWX5P6wuzGN_gz11oS99qbWq_lajxkMHrKM8R0d2LsD-xn8V4-x09s6Omwa06Lvo-aU0kFhQcWAzg6oCz7GgNVxm4IehetRuB6F61H4ULj92-7tFssj_m-Y_wCwcn4P |
| Cites_doi | 10.1038/ncomms4978 10.1093/nar/gkw1041 10.1016/j.bbalip.2016.04.004 10.1264/jsme2.ME23093 10.1104/pp.19.01246 10.1111/jpy.13238 10.1016/j.algal.2020.101990 10.1038/s41586-019-1693-2 10.1111/j.1574-6976.2012.00351.x 10.1080/10635150290069913 10.1186/1471-2164-15-582 10.1038/s42003-022-03939-z 10.1016/j.mib.2005.02.011 10.1038/s43705-023-00284-y 10.1104/pp.001842 10.1073/pnas.1703088114 10.1104/pp.18.00216 10.1093/molbev/msx281 10.1038/nature11241 10.1038/s41467-022-35566-x 10.1093/nar/gkr1090 10.1093/nar/gkf436 10.1371/journal.pone.0131099 10.1105/tpc.114.124982 10.1093/dnares/dsm026 10.1093/nar/gkac1000 10.3390/toxins12040248 10.1016/j.cell.2019.10.019 10.1016/j.tim.2021.12.014 10.1128/genomeA.01448-17 10.1111/nph.18662 10.1073/pnas.0910097107 10.1111/tpj.13801 10.1093/plcell/koac347 10.1016/j.tplants.2010.10.004 10.1073/pnas.1619928114 10.1146/annurev.arplant.53.100301.135251 10.1186/gb-2012-13-5-r39 10.1093/molbev/msaa015 10.1074/jbc.RA120.012877 10.1016/S0003-9861(02)00025-5 10.1073/pnas.1221259110 10.1038/s41588-024-01737-3 10.1016/j.ecolind.2023.111171 10.3389/fmolb.2020.615614 10.1104/pp.125.4.2016 10.1128/MRA.00750-19 10.1126/science.1188800 10.3109/07388551.2012.668671 10.1104/pp.18.01584 10.1016/j.plantsci.2021.111130 10.1128/genomeA.00215-17 10.1111/mmi.12912 10.1038/s41467-020-20014-5 10.1104/pp.110.165910 10.1105/tpc.16.00317 10.1038/s41477-022-01226-7 10.1073/pnas.1016106108 10.1111/tpj.15632 10.1006/mben.2001.0204 10.1021/bi0520479 10.3389/fpls.2020.589026 10.7554/eLife.45017 10.1002/ece3.10873 10.1104/pp.113.1.75 10.1093/molbev/msac171 10.1016/S0163-7827(02)00007-3 10.1104/pp.108.134882 10.1126/science.1203810 10.1093/sysbio/syq010 10.1038/nmeth.4285 10.1016/S0021-9258(19)42203-5 10.1016/j.cub.2021.01.018 |
| ContentType | Journal Article |
| Copyright | Distributed under a Creative Commons Attribution 4.0 International License |
| Copyright_xml | – notice: Distributed under a Creative Commons Attribution 4.0 International License |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 1XC |
| DOI | 10.1098/rstb.2023.0353 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic Hyper Article en Ligne (HAL) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE 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 | Medicine Sciences (General) Biology |
| EISSN | 1471-2970 |
| ExternalDocumentID | oai_HAL_hal_04715523v1 10_1098_rstb_2023_0353 39343023 |
| Genre | Journal Article Review |
| GrantInformation_xml | – fundername: National Science Foundation – fundername: Department of Energy Office of Biological and Environmental Research (BER) |
| GroupedDBID | --- -~X 0R~ 2WC 4.4 53G AACGO AANCE ABPLY ABTLG ACPRK ADBBV AEUPB AFRAH ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BTFSW CGR CUY CVF E3Z EBS ECM EIF F5P GX1 HZ~ JSG KQ8 MRS MV1 NPM NSAHA O9- OK1 OP1 RPM RRY TN5 V1E YNT ~02 AAYXX CITATION 7X8 1XC |
| ID | FETCH-LOGICAL-c1293-e64cfd9cd07c89bbb778e5007d7bce1ab20026a274de5617f49dbd0c70cc244b3 |
| ISSN | 0962-8436 1471-2970 |
| IngestDate | Wed Oct 02 06:35:28 EDT 2024 Mon Sep 30 17:01:16 EDT 2024 Wed Oct 02 14:36:06 EDT 2024 Wed Oct 02 05:28:27 EDT 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1914 |
| Keywords | ACCase fatty acid synthesis acetyl-CoA carboxylase metabolic regulation |
| Language | English |
| License | Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c1293-e64cfd9cd07c89bbb778e5007d7bce1ab20026a274de5617f49dbd0c70cc244b3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| ORCID | 0000-0002-8608-8546 0000-0003-1064-1816 |
| PMID | 39343023 |
| PQID | 3111202814 |
| PQPubID | 23479 |
| ParticipantIDs | hal_primary_oai_HAL_hal_04715523v1 proquest_miscellaneous_3111202814 crossref_primary_10_1098_rstb_2023_0353 pubmed_primary_39343023 |
| PublicationCentury | 2000 |
| PublicationDate | 2024-Nov-18 |
| PublicationDateYYYYMMDD | 2024-11-18 |
| PublicationDate_xml | – month: 11 year: 2024 text: 2024-Nov-18 day: 18 |
| PublicationDecade | 2020 |
| PublicationPlace | England |
| PublicationPlace_xml | – name: England |
| PublicationTitle | Philosophical transactions of the Royal Society of London. Series B. Biological sciences |
| PublicationTitleAlternate | Philos Trans R Soc Lond B Biol Sci |
| PublicationYear | 2024 |
| Publisher | Royal Society, The |
| Publisher_xml | – name: Royal Society, The |
| References | e_1_3_7_62_2 e_1_3_7_60_2 e_1_3_7_20_2 e_1_3_7_43_2 e_1_3_7_66_2 e_1_3_7_22_2 e_1_3_7_41_2 e_1_3_7_64_2 e_1_3_7_24_2 e_1_3_7_47_2 e_1_3_7_26_2 e_1_3_7_45_2 e_1_3_7_68_2 e_1_3_7_28_2 e_1_3_7_49_2 Peng C (e_1_3_7_72_2) 2015; 169 e_1_3_7_51_2 e_1_3_7_70_2 e_1_3_7_30_2 e_1_3_7_55_2 e_1_3_7_76_2 e_1_3_7_11_2 e_1_3_7_32_2 e_1_3_7_53_2 e_1_3_7_74_2 e_1_3_7_13_2 e_1_3_7_34_2 e_1_3_7_59_2 e_1_3_7_15_2 e_1_3_7_36_2 e_1_3_7_57_2 e_1_3_7_17_2 e_1_3_7_38_2 e_1_3_7_19_2 e_1_3_7_2_2 e_1_3_7_4_2 e_1_3_7_6_2 e_1_3_7_8_2 e_1_3_7_61_2 e_1_3_7_40_2 e_1_3_7_65_2 e_1_3_7_44_2 e_1_3_7_63_2 e_1_3_7_21_2 e_1_3_7_42_2 e_1_3_7_23_2 e_1_3_7_48_2 e_1_3_7_69_2 e_1_3_7_25_2 e_1_3_7_46_2 e_1_3_7_67_2 e_1_3_7_27_2 e_1_3_7_29_2 e_1_3_7_9_2 e_1_3_7_50_2 e_1_3_7_73_2 e_1_3_7_71_2 e_1_3_7_31_2 e_1_3_7_54_2 e_1_3_7_77_2 e_1_3_7_10_2 e_1_3_7_33_2 e_1_3_7_52_2 e_1_3_7_75_2 e_1_3_7_12_2 e_1_3_7_35_2 e_1_3_7_58_2 e_1_3_7_14_2 e_1_3_7_37_2 e_1_3_7_56_2 e_1_3_7_16_2 e_1_3_7_39_2 e_1_3_7_18_2 e_1_3_7_3_2 e_1_3_7_5_2 e_1_3_7_7_2 |
| References_xml | – ident: e_1_3_7_25_2 doi: 10.1038/ncomms4978 – volume: 169 start-page: 1807 year: 2015 ident: e_1_3_7_72_2 article-title: The impact of the branched-chain ketoacid dehydrogenase complex on amino acid homeostasis in Arabidopsis publication-title: Plant Physiol. contributor: fullname: Peng C – ident: e_1_3_7_58_2 doi: 10.1093/nar/gkw1041 – ident: e_1_3_7_4_2 doi: 10.1016/j.bbalip.2016.04.004 – ident: e_1_3_7_34_2 doi: 10.1264/jsme2.ME23093 – ident: e_1_3_7_68_2 doi: 10.1104/pp.19.01246 – ident: e_1_3_7_40_2 doi: 10.1111/jpy.13238 – ident: e_1_3_7_30_2 doi: 10.1016/j.algal.2020.101990 – ident: e_1_3_7_76_2 doi: 10.1038/s41586-019-1693-2 – ident: e_1_3_7_11_2 doi: 10.1111/j.1574-6976.2012.00351.x – ident: e_1_3_7_52_2 doi: 10.1080/10635150290069913 – ident: e_1_3_7_26_2 doi: 10.1186/1471-2164-15-582 – ident: e_1_3_7_35_2 doi: 10.1038/s42003-022-03939-z – ident: e_1_3_7_9_2 doi: 10.1016/j.mib.2005.02.011 – ident: e_1_3_7_46_2 doi: 10.1038/s43705-023-00284-y – ident: e_1_3_7_71_2 doi: 10.1104/pp.001842 – ident: e_1_3_7_41_2 doi: 10.1073/pnas.1703088114 – ident: e_1_3_7_14_2 doi: 10.1104/pp.18.00216 – ident: e_1_3_7_54_2 doi: 10.1093/molbev/msx281 – ident: e_1_3_7_18_2 doi: 10.1038/nature11241 – ident: e_1_3_7_43_2 doi: 10.1038/s41467-022-35566-x – ident: e_1_3_7_17_2 doi: 10.1093/nar/gkr1090 – ident: e_1_3_7_50_2 doi: 10.1093/nar/gkf436 – ident: e_1_3_7_60_2 doi: 10.1371/journal.pone.0131099 – ident: e_1_3_7_74_2 doi: 10.1105/tpc.114.124982 – ident: e_1_3_7_44_2 doi: 10.1093/dnares/dsm026 – ident: e_1_3_7_57_2 doi: 10.1093/nar/gkac1000 – ident: e_1_3_7_45_2 doi: 10.3390/toxins12040248 – ident: e_1_3_7_23_2 doi: 10.1016/j.cell.2019.10.019 – ident: e_1_3_7_66_2 doi: 10.1016/j.tim.2021.12.014 – ident: e_1_3_7_37_2 doi: 10.1128/genomeA.01448-17 – ident: e_1_3_7_24_2 doi: 10.1111/nph.18662 – ident: e_1_3_7_10_2 doi: 10.1073/pnas.0910097107 – ident: e_1_3_7_21_2 doi: 10.1111/tpj.13801 – ident: e_1_3_7_31_2 doi: 10.1093/plcell/koac347 – ident: e_1_3_7_67_2 doi: 10.1016/j.tplants.2010.10.004 – ident: e_1_3_7_29_2 doi: 10.1073/pnas.1619928114 – ident: e_1_3_7_61_2 doi: 10.1146/annurev.arplant.53.100301.135251 – ident: e_1_3_7_28_2 doi: 10.1186/gb-2012-13-5-r39 – ident: e_1_3_7_51_2 doi: 10.1093/molbev/msaa015 – ident: e_1_3_7_7_2 doi: 10.1074/jbc.RA120.012877 – ident: e_1_3_7_16_2 doi: 10.1016/S0003-9861(02)00025-5 – ident: e_1_3_7_39_2 doi: 10.1073/pnas.1221259110 – ident: e_1_3_7_22_2 doi: 10.1038/s41588-024-01737-3 – ident: e_1_3_7_49_2 doi: 10.1016/j.ecolind.2023.111171 – ident: e_1_3_7_15_2 doi: 10.3389/fmolb.2020.615614 – ident: e_1_3_7_64_2 doi: 10.1104/pp.125.4.2016 – ident: e_1_3_7_38_2 doi: 10.1128/MRA.00750-19 – ident: e_1_3_7_32_2 doi: 10.1126/science.1188800 – ident: e_1_3_7_59_2 doi: 10.3109/07388551.2012.668671 – ident: e_1_3_7_73_2 doi: 10.1104/pp.18.01584 – ident: e_1_3_7_70_2 doi: 10.1016/j.plantsci.2021.111130 – ident: e_1_3_7_27_2 doi: 10.1128/genomeA.00215-17 – ident: e_1_3_7_6_2 doi: 10.1111/mmi.12912 – ident: e_1_3_7_8_2 doi: 10.1038/s41467-020-20014-5 – ident: e_1_3_7_65_2 doi: 10.1104/pp.110.165910 – ident: e_1_3_7_12_2 doi: 10.1105/tpc.16.00317 – ident: e_1_3_7_19_2 doi: 10.1038/s41477-022-01226-7 – ident: e_1_3_7_36_2 doi: 10.1073/pnas.1016106108 – ident: e_1_3_7_69_2 doi: 10.1111/tpj.15632 – ident: e_1_3_7_77_2 – ident: e_1_3_7_2_2 doi: 10.1006/mben.2001.0204 – ident: e_1_3_7_63_2 doi: 10.1021/bi0520479 – ident: e_1_3_7_75_2 doi: 10.3389/fpls.2020.589026 – ident: e_1_3_7_42_2 doi: 10.7554/eLife.45017 – ident: e_1_3_7_48_2 doi: 10.3390/toxins12040248 – ident: e_1_3_7_56_2 doi: 10.1002/ece3.10873 – ident: e_1_3_7_5_2 doi: 10.1104/pp.113.1.75 – ident: e_1_3_7_47_2 doi: 10.1093/molbev/msac171 – ident: e_1_3_7_62_2 doi: 10.1016/S0163-7827(02)00007-3 – ident: e_1_3_7_13_2 doi: 10.1104/pp.108.134882 – ident: e_1_3_7_20_2 doi: 10.1126/science.1203810 – ident: e_1_3_7_53_2 doi: 10.1093/sysbio/syq010 – ident: e_1_3_7_55_2 doi: 10.1038/nmeth.4285 – ident: e_1_3_7_3_2 doi: 10.1016/S0021-9258(19)42203-5 – ident: e_1_3_7_33_2 doi: 10.1016/j.cub.2021.01.018 |
| SSID | ssj0009574 |
| Score | 2.496991 |
| SecondaryResourceType | review_article |
| Snippet | The committed step for de novo fatty acid (FA) synthesis is the ATP-dependent carboxylation of acetyl-coenzyme A catalysed by acetyl-CoA carboxylase (ACCase).... |
| SourceID | hal proquest crossref pubmed |
| SourceType | Open Access Repository Aggregation Database Index Database |
| StartPage | 20230353 |
| SubjectTerms | Acetyl-CoA Carboxylase - genetics Acetyl-CoA Carboxylase - metabolism Arabidopsis - enzymology Arabidopsis - genetics Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - genetics Evolution, Molecular Life Sciences |
| Title | Evolution of the regulatory subunits for the heteromeric acetyl-CoA carboxylase |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/39343023 https://www.proquest.com/docview/3111202814/abstract/ https://hal.science/hal-04715523 |
| Volume | 379 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1tb9MwELbKEIgviBUY5U0BIQFCCWnsvH0sZVPZujHGJvVbZDuOijQlaE0myl_kT3EXx0kqhjT4ElVO6zi-6_nse-4eQl6JLI6FkIGtMi-0GaOpLaQrbQZbDeExpaTABOfDo2B2xvYX_mIw-NVDLVWlcOTPK_NK_keq0AZyxSzZf5Bs2yk0wGeQL1xBwnC9lox3L5vuTaT_QjPLY9x8VYkqx6iAwREuEfhSaOg8l6pcn9vTYoKlqUXxY31uojSNo3psKA5qIZYdq_jKPEsfPBjUJ4YaamYQB80PbL_ffXAaossu8VJ2gMUp0hqkOscm5xp30gvxzxUWkdrH8_r65J4L6LMFg5zw-ocnjmlYVBo6UOXL6lv_IMNjmNHX2F6NgOqNWiOkVP-4MgDLzWhTNlsba1hYbS_WxCPGmlPNTWPUNtYpqn8sFG6MyQ_gYAsHCeQdl-qaxZsVuWeTr8nxx71k_unoYPNuW5p7NpknS9AcFwbjw67-ErbiN70w9vEk4OBL1KsArUuCmxdpK4hG7zeHseEh3VgiPvdvm5_aCTq9R-42uxdrolVxmwxUPiS3tJjXQ3L7sEFqDMl2s2isrDdNZfO398nnVmGtIrNAiaxOYS2jsBYobH2vp7BWp7BWT2EfkLO93dPpzG4YPWyJfqWtAiazNJapG8oIbIQIw0j54KamoZBqzAVChgLuhSxV4NiHGYtTkboydKUEP1TQh2QrL3L1iFgYYGZIPzDmIQsE0ijwsZv5POWCUeqPyGszi8l3Xbgl0YCLKMH5TnC-E5zvEXmJAjRfulqoI_LCyCABA4xRNZ6rololFLwF6CsasxHZ0cJp-6IxZcjK9fg6j3hC7nR_i6dkq7yo1DPweEvxvNak30DYrnk |
| link.rule.ids | 230,315,786,790,891,27957,27958 |
| linkProvider | Colorado Alliance of Research Libraries |
| 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=Evolution+of+the+regulatory+subunits+for+the+heteromeric+acetyl-CoA+carboxylase&rft.jtitle=Philosophical+transactions+of+the+Royal+Society+of+London.+Series+B.+Biological+sciences&rft.au=Conrado%2C+Ana+Caroline&rft.au=Lemes+Jorge%2C+Gabriel&rft.au=Rao%2C+R.&rft.au=Xu%2C+Chunhui&rft.date=2024-11-18&rft.pub=Royal+Society%2C+The&rft.issn=0962-8436&rft.eissn=1471-2970&rft.volume=379&rft.issue=1914&rft_id=info:doi/10.1098%2Frstb.2023.0353&rft.externalDBID=HAS_PDF_LINK&rft.externalDocID=oai_HAL_hal_04715523v1 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0962-8436&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0962-8436&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0962-8436&client=summon |