标题
Disruption of divisome assembly rescued by FtsN–FtsA interaction inEscherichia coli
作者
关键词
-
出版物
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 29, Pages E6855-E6862
出版商
Proceedings of the National Academy of Sciences
发表日期
2018-07-03
DOI
10.1073/pnas.1806450115
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division
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- Splitsville: structural and functional insights into the dynamic bacterial Z ring
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- FtsEX acts on FtsA to regulate divisome assembly and activity
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- Guiding divisome assembly and controlling its activity
- (2015) Mary-Jane Tsang et al. CURRENT OPINION IN MICROBIOLOGY
- The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring
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- Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction inEscherichia coli
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- Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides
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- A role for FtsA in SPOR-independent localization of the essentialEscherichia colicell division protein FtsN
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- Identification of SPOR Domain Amino Acids Important for Septal Localization, Peptidoglycan Binding, and a Disulfide Bond in the Cell Division Protein FtsN
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- Bacterial cytokinesis: From Z ring to divisome
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- FtsA forms actin-like protofilaments
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- The Early Divisome Protein FtsA Interacts Directly through Its 1c Subdomain with the Cytoplasmic Domain of the Late Divisome Protein FtsN
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- FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
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- An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
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- Self-Enhanced Accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR Domain (DamX, DedD, and RlpA) in Escherichia coli Cell Constriction
- (2009) M. A. Gerding et al. JOURNAL OF BACTERIOLOGY
- FtsN--Trigger for Septation
- (2009) J. Lutkenhaus JOURNAL OF BACTERIOLOGY
- ATP-Binding Site Lesions in FtsE Impair Cell Division
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- The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure
- (2008) Michael Tarry et al. JOURNAL OF MOLECULAR BIOLOGY
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