GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis

被引:321
|
作者
Yang, Xinxing [1 ]
Lyu, Zhixin [1 ]
Miguel, Amanda [2 ]
McQuillen, Ryan [1 ]
Huang, Kerwyn Casey [2 ,3 ]
Xiao, Jie [1 ]
机构
[1] Johns Hopkins Univ, Dept Biophys & Biophys Chem, Sch Med, Baltimore, MD 21205 USA
[2] Stanford Univ, Dept Bioengn, Stanford, CA 94305 USA
[3] Stanford Univ, Dept Microbiol & Immunol, Sch Med, Stanford, CA 94305 USA
关键词
DIVISION PROTEIN FTSZ; Z-RING STRUCTURE; SUPERRESOLUTION; PEPTIDOGLYCAN; MUTATIONS; DYNAMICS; MUTANTS; BINDING;
D O I
10.1126/science.aak9995
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The bacterial tubulin FtsZ is the central component of the cell division machinery, coordinating an ensemble of proteins involved in septal cell wall synthesis to ensure successful constriction. How cells achieve this coordination is unknown. We found that in Escherichia coli cells, FtsZ exhibits dynamic treadmilling predominantly determined by its guanosine triphosphatase activity. The treadmilling dynamics direct the processive movement of the septal cell wall synthesis machinery but do not limit the rate of septal synthesis. In FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall were substantially altered. Thus, FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology.
引用
收藏
页码:744 / +
页数:5
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