| FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. | |
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MedLine Citation:
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PMID: 15466028 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The mechanisms by which bacteria adopt and maintain individual shapes remain enigmatic. Outstanding questions include why cells are a certain size, length, and width; why they are uniform or irregular; and why some branch while others do not. Previously, we showed that Escherichia coli mutants lacking multiple penicillin binding proteins (PBPs) display extensive morphological diversity. Because defective sites in these cells exhibit the structural and functional characteristics of improperly localized poles, we investigated the connection between cell division and shape. Here we show that under semipermissive conditions the temperature-sensitive FtsZ84 protein produces branched and aberrant cells at a high frequency in mutants lacking PBP 5, and this phenotype is exacerbated by the loss of additional peptidoglycan endopeptidases. Surprisingly, certain ftsZ84 strains lyse at the nonpermissive temperature instead of filamenting, and inhibition of wild-type FtsZ forces some mutants into tightly wound spirillum-like morphologies. The results demonstrate that significant aspects of bacterial shape are dictated by a previously unrecognized relationship between the septation machinery and ostensibly minor peptidoglycan-modifying enzymes and that under certain circumstances improper FtsZ function can destroy the structural integrity of the cell. |
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Authors:
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Archana Varma; Kevin D Young |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of bacteriology Volume: 186 ISSN: 0021-9193 ISO Abbreviation: J. Bacteriol. Publication Date: 2004 Oct |
Date Detail:
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Created Date: 2004-10-06 Completed Date: 2004-11-02 Revised Date: 2011-01-04 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 6768-74 Citation Subset: IM |
Affiliation:
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Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202, USA. kyoung@medicine.nodak.edu. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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metabolism* Bacteriolysis Carrier Proteins / metabolism* Escherichia coli / cytology*, genetics, physiology Escherichia coli Proteins / genetics, metabolism* Gene Expression Regulation, Bacterial* Hexosyltransferases / metabolism* Microscopy, Electron, Scanning Muramoylpentapeptide Carboxypeptidase / metabolism* Mutagenesis, Site-Directed Mutation Penicillin-Binding Proteins Peptidyl Transferases / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM61019/GM/NIGMS NIH HHS; R01 GM061019-05/GM/NIGMS NIH HHS; R01 GM061019-06/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Carrier Proteins; 0/Escherichia coli Proteins; 0/FtsZ84 protein, E coli; 0/Penicillin-Binding Proteins; EC 2.3.2.12/Peptidyl Transferases; EC 2.4.1.-/Hexosyltransferases; EC 3.4.17.8/Muramoylpentapeptide Carboxypeptidase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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