Document Detail


Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes.
MedLine Citation:
PMID:  22509007     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell division in typical rod-shaped bacteria such as Escherichia coli shows a remarkable plasticity in being able to adapt to a variety of irregular cell shapes. Here, we investigate the roles of the Min system and the nucleoid-occlusion factor SlmA in supporting this adaptation. We study "squeezed" E. coli in narrow nanofabricated channels where these bacteria exhibit highly irregular shapes and large volumes. Despite the severely anomalous morphologies we find that most of these bacteria maintain their ability to divide into two equally sized daughters with an accuracy comparable to that of normal rod-shaped cells (about 4%). Deletion of either slmA or minC shows that the molecular systems associated with these genes are largely dispensable for accurate cell division in these irregular cell shapes. Using fluorescence time-lapse microscopy, we determine that the functionality of the Min system is affected by the cell shape, whereas the localization of a nucleoid relative to the cell division proteins (the divisome) remains unperturbed in a broad spectrum of morphologies, consistent with nucleoid occlusion. The observed positioning of the nucleoid relative to the divisome appears not to be affected by the nucleoid-occlusion factor SlmA. The current study underscores the importance of nucleoid occlusion in positioning the divisome and shows that it is robust against shape irregularities.
Authors:
Jaan Männik; Fabai Wu; Felix J H Hol; Paola Bisicchia; David J Sherratt; Juan E Keymer; Cees Dekker
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-04-16
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-05-02     Completed Date:  2012-07-10     Revised Date:  2014-07-16    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6957-62     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / genetics,  physiology
Bacterial Proteins / genetics,  physiology
Biophysical Phenomena
Carrier Proteins / genetics,  physiology
Cell Division / genetics,  physiology*
Cytoskeletal Proteins / genetics,  physiology
Escherichia coli K12 / cytology*,  genetics,  physiology*
Escherichia coli Proteins / genetics,  physiology
Gene Deletion
Genes, Bacterial
Green Fluorescent Proteins / genetics,  metabolism
Membrane Proteins / genetics,  physiology
Microfluidic Analytical Techniques / instrumentation
Microscopy, Fluorescence
Recombinant Fusion Proteins / genetics,  metabolism
Time-Lapse Imaging
Grant Support
ID/Acronym/Agency:
091911//Wellcome Trust; 247072//European Research Council
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Carrier Proteins; 0/Cytoskeletal Proteins; 0/Escherichia coli Proteins; 0/FtsZ protein, Bacteria; 0/Membrane Proteins; 0/MinC protein, E coli; 0/Recombinant Fusion Proteins; 0/SlmA protein, E coli; 0/hupA protein, E coli; 147336-22-9/Green Fluorescent Proteins; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/MinD protein, E coli
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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