2011
DOI: 10.1128/jb.01258-10
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Abstract: In Escherichia coli, spatiotemporal control of cell division occurs at the level of the assembly/disassembly process of the essential cytoskeletal protein FtsZ. A number of regulators interact with FtsZ and modulate the dynamics of the assembled FtsZ ring at the midcell division site. In this article, we report the identification of an FtsZ stabilizer, ZapC (Z-associated protein C), in a protein localization screen conducted with E. coli. ZapC colocalizes with FtsZ at midcell and interacts directly with FtsZ, … Show more

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Cited by 91 publications
(106 citation statements)
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“…The assembly and stabilization of FtsZ polymers in the proto-ring are regulated by the Zap proteins (ZapA, ZapB, ZapC, and ZapD), which exhibit functionally redundant roles in binding and bundling polymeric FtsZ (32,[40][41][42][43][44][45][46]. These proteins act at midcell, promoting the transition of FtsZ polymers from a helical band into a compact ring by cooperatively stimulating the lateral association of protofilaments (47, 48).…”
Section: The Proto-ring: the Scaffold Of The Divisomementioning
confidence: 99%
“…The assembly and stabilization of FtsZ polymers in the proto-ring are regulated by the Zap proteins (ZapA, ZapB, ZapC, and ZapD), which exhibit functionally redundant roles in binding and bundling polymeric FtsZ (32,[40][41][42][43][44][45][46]. These proteins act at midcell, promoting the transition of FtsZ polymers from a helical band into a compact ring by cooperatively stimulating the lateral association of protofilaments (47, 48).…”
Section: The Proto-ring: the Scaffold Of The Divisomementioning
confidence: 99%
“…Once established, the Z-ring recruits an ensemble of transmembrane and periplasmic proteins involved in cell wall peptidoglycan (PG) synthesis and remodeling, including the essential transpeptidase and penicillinbinding protein PBP3 (also called FtsI) (8,9). Recently, a new group of Z-ring-associated proteins (Zaps) has been shown to stabilize the Z-ring (10)(11)(12)(13)(14)(15). Some of these Zaps connect the Z-ring to the bacterial chromosome through a multilayered protein network that includes the chromosome-binding protein MatP (16)(17)(18)(19).…”
mentioning
confidence: 99%
“…In E. coli, this process is mediated by FtsZ-associated proteins (Zap proteins). The first Zap proteins recruited during divisome assembly are ZapA, ZapB, ZapC, and ZapD and are predicted to have overlapping functions (17)(18)(19)(20)(21). These Zap proteins stabilize FtsZ filaments prior to cell division by slowing depolymerization, thereby inhibiting GTPase activity (17,19,21,22).…”
mentioning
confidence: 99%
“…The first Zap proteins recruited during divisome assembly are ZapA, ZapB, ZapC, and ZapD and are predicted to have overlapping functions (17)(18)(19)(20)(21). These Zap proteins stabilize FtsZ filaments prior to cell division by slowing depolymerization, thereby inhibiting GTPase activity (17,19,21,22). It has recently been shown that a fifth Zap protein, ZapE, also functions during division; however, it is thought to have a function opposing that of ZapA, ZapB, ZapC, and ZapD, as it binds to and causes the dissociation of FtsZ filaments (23).…”
mentioning
confidence: 99%