DOI: 10.1073/pnas.1806450115
论文题名: Disruption of divisome assembly rescued by FtsN–FtsA interaction in Escherichia coli
作者: Pichoff S. ; Du S. ; Lutkenhaus J.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期: 29 起始页码: E6855
结束页码: E6862
语种: 英语
英文关键词: 0.1073/pnas.1806450115
; Divisome
; FtsA
; FtsN
; FtsZ
; Z-ring
Scopus关键词: divisome protein
; divisome protein FtsA
; divisome protein FtsEX
; divisome protein FtsN
; protein
; unclassified drug
; ABC transporter
; cell cycle protein
; cystic fibrosis transmembrane conductance regulator
; Escherichia coli protein
; FtsA protein, E coli
; FtsE protein, E coli
; FtsN protein, E coli
; FtsX protein, E coli
; membrane protein
; Article
; controlled study
; delta ftsEX gene
; delta ftsK gene
; Escherichia coli
; ftsA gene
; gene
; gene overexpression
; nonhuman
; periplasm
; physiology
; priority journal
; protein assembly
; protein protein interaction
; cell division
; Escherichia coli
; genetics
; metabolism
; physiology
; ATP-Binding Cassette Transporters
; Cell Cycle Proteins
; Cell Division
; Cystic Fibrosis Transmembrane Conductance Regulator
; Escherichia coli
; Escherichia coli Proteins
; Membrane Proteins
; Periplasm
英文摘要: Cell division requires the assembly of a protein complex called the divisome. The divisome assembles in a hierarchical manner, with FtsA functioning as a hub to connect the Z-ring with the rest of the divisome and FtsN arriving last to activate the machine to synthesize peptidoglycan. FtsEX arrives as the Z-ring forms and acts on FtsA to initiate recruitment of the other divisome components. In the absence of FtsEX, recruitment is blocked; however, a multitude of conditions allow FtsEX to be bypassed. Here, we find that all such FtsEX bypass conditions, as well as the bypass of FtsK, depend upon the interaction of FtsN with FtsA, which promotes the back-recruitment of the late components of the divisome. Furthermore, our results suggest that these bypass conditions enhance the weak interaction of FtsN with FtsA and its periplasmic partners so that the divisome proteins are brought to the Z-ring when the normal hierarchical pathway is disrupted. © 2018 National Academy of Sciences. All Rights Reserved. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163690
Appears in Collections: 气候变化与战略
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作者单位: Pichoff, S., Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, United States; Du, S., Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, United States; Lutkenhaus, J., Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, United States
Recommended Citation:
Pichoff S.,Du S.,Lutkenhaus J.. Disruption of divisome assembly rescued by FtsN–FtsA interaction in Escherichia coli[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(29)