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Title: Dynamic nature of SecA and its associated proteins in Escherichia coli.
Authors: Adachi, Shun
Murakawa, Yasuhiro  kyouindb  KAKEN_id  orcid (unconfirmed)
Hiraga, Sota
Author's alias: 足立, 隼
村川, 泰裕
平賀, 壯太
Keywords: chromosome partition
DNA topoisomerase
Issue Date: 10-Feb-2015
Publisher: Frontiers
Journal title: Frontiers in microbiology
Volume: 6
Thesis number: 75
Abstract: 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).
Rights: © 2015 Adachi, Murakawa and Hiraga. 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.
DOI(Published Version): 10.3389/fmicb.2015.00075
PubMed ID: 25713567
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