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Dynamic nature of SecA and its associated proteins in Escherichia coli
Mechanical properties such as physical constraint and pushing of chromosomes are thought to be important for chromosome segregation in Escherichia coli and it could be mediated by a hypothetical molecular “tether.” However, the actual tether that mediates these features is not known. We previously d...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4322705/ https://www.ncbi.nlm.nih.gov/pubmed/25713567 http://dx.doi.org/10.3389/fmicb.2015.00075 |
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author | Adachi, Shun Murakawa, Yasuhiro Hiraga, Sota |
author_facet | Adachi, Shun Murakawa, Yasuhiro Hiraga, Sota |
author_sort | Adachi, Shun |
collection | PubMed |
description | Mechanical properties such as physical constraint and pushing of chromosomes are thought to be important for chromosome segregation in Escherichia coli and it could be mediated by a hypothetical molecular “tether.” However, the actual tether that mediates these features is not known. We previously described that SecA (Secretory A) and Secretory Y (SecY), components of the membrane protein translocation machinery, and AcpP (Acyl carrier protein P) were involved in chromosome segregation and homeostasis of DNA topology. In the present work, we performed three-dimensional deconvolution of microscopic images and time-lapse experiments of these proteins together with MukB and DNA topoisomerases, and found that these proteins embraced the structures of tortuous nucleoids with condensed regions. Notably, SecA, SecY, and AcpP dynamically localized in cells, which was interdependent on each other requiring the ATPase activity of SecA. Our findings imply that the membrane protein translocation machinery plays a role in the maintenance of proper chromosome partitioning, possibly through “tethering” of MukB [a functional homolog of structural maintenance of chromosomes (SMC) proteins], DNA gyrase, DNA topoisomerase IV, and SeqA (Sequestration A). |
format | Online Article Text |
id | pubmed-4322705 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-43227052015-02-24 Dynamic nature of SecA and its associated proteins in Escherichia coli Adachi, Shun Murakawa, Yasuhiro Hiraga, Sota Front Microbiol Microbiology Mechanical properties such as physical constraint and pushing of chromosomes are thought to be important for chromosome segregation in Escherichia coli and it could be mediated by a hypothetical molecular “tether.” However, the actual tether that mediates these features is not known. We previously described that SecA (Secretory A) and Secretory Y (SecY), components of the membrane protein translocation machinery, and AcpP (Acyl carrier protein P) were involved in chromosome segregation and homeostasis of DNA topology. In the present work, we performed three-dimensional deconvolution of microscopic images and time-lapse experiments of these proteins together with MukB and DNA topoisomerases, and found that these proteins embraced the structures of tortuous nucleoids with condensed regions. Notably, SecA, SecY, and AcpP dynamically localized in cells, which was interdependent on each other requiring the ATPase activity of SecA. Our findings imply that the membrane protein translocation machinery plays a role in the maintenance of proper chromosome partitioning, possibly through “tethering” of MukB [a functional homolog of structural maintenance of chromosomes (SMC) proteins], DNA gyrase, DNA topoisomerase IV, and SeqA (Sequestration A). Frontiers Media S.A. 2015-02-10 /pmc/articles/PMC4322705/ /pubmed/25713567 http://dx.doi.org/10.3389/fmicb.2015.00075 Text en Copyright © 2015 Adachi, Murakawa and Hiraga. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Adachi, Shun Murakawa, Yasuhiro Hiraga, Sota Dynamic nature of SecA and its associated proteins in Escherichia coli |
title | Dynamic nature of SecA and its associated proteins in Escherichia coli |
title_full | Dynamic nature of SecA and its associated proteins in Escherichia coli |
title_fullStr | Dynamic nature of SecA and its associated proteins in Escherichia coli |
title_full_unstemmed | Dynamic nature of SecA and its associated proteins in Escherichia coli |
title_short | Dynamic nature of SecA and its associated proteins in Escherichia coli |
title_sort | dynamic nature of seca and its associated proteins in escherichia coli |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4322705/ https://www.ncbi.nlm.nih.gov/pubmed/25713567 http://dx.doi.org/10.3389/fmicb.2015.00075 |
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