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Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation
Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular co...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8602292/ https://www.ncbi.nlm.nih.gov/pubmed/34795302 http://dx.doi.org/10.1038/s41467-021-27107-9 |
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author | Prince, Josh P. Bolla, Jani R. Fisher, Gemma L. M. Mäkelä, Jarno Fournier, Marjorie Robinson, Carol V. Arciszewska, Lidia K. Sherratt, David J. |
author_facet | Prince, Josh P. Bolla, Jani R. Fisher, Gemma L. M. Mäkelä, Jarno Fournier, Marjorie Robinson, Carol V. Arciszewska, Lidia K. Sherratt, David J. |
author_sort | Prince, Josh P. |
collection | PubMed |
description | Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE proteins that interact with kleisins. The ATPase activity of the Escherichia coli SMC protein, MukB, which is essential for its in vivo function, requires its interaction with the dimeric kleisin, MukF that in turn interacts with the KITE protein, MukE. Here we demonstrate that, in addition, MukB interacts specifically with Acyl Carrier Protein (AcpP) that has essential functions in fatty acid synthesis. We characterize the AcpP interaction at the joint of the MukB coiled-coil and show that the interaction is necessary for MukB ATPase and for MukBEF function in vivo. |
format | Online Article Text |
id | pubmed-8602292 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-86022922021-11-19 Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation Prince, Josh P. Bolla, Jani R. Fisher, Gemma L. M. Mäkelä, Jarno Fournier, Marjorie Robinson, Carol V. Arciszewska, Lidia K. Sherratt, David J. Nat Commun Article Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE proteins that interact with kleisins. The ATPase activity of the Escherichia coli SMC protein, MukB, which is essential for its in vivo function, requires its interaction with the dimeric kleisin, MukF that in turn interacts with the KITE protein, MukE. Here we demonstrate that, in addition, MukB interacts specifically with Acyl Carrier Protein (AcpP) that has essential functions in fatty acid synthesis. We characterize the AcpP interaction at the joint of the MukB coiled-coil and show that the interaction is necessary for MukB ATPase and for MukBEF function in vivo. Nature Publishing Group UK 2021-11-18 /pmc/articles/PMC8602292/ /pubmed/34795302 http://dx.doi.org/10.1038/s41467-021-27107-9 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Prince, Josh P. Bolla, Jani R. Fisher, Gemma L. M. Mäkelä, Jarno Fournier, Marjorie Robinson, Carol V. Arciszewska, Lidia K. Sherratt, David J. Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title | Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title_full | Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title_fullStr | Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title_full_unstemmed | Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title_short | Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation |
title_sort | acyl carrier protein promotes mukbef action in escherichia coli chromosome organization-segregation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8602292/ https://www.ncbi.nlm.nih.gov/pubmed/34795302 http://dx.doi.org/10.1038/s41467-021-27107-9 |
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