The ClpX chaperone modulates assembly of the tubulin‐like protein FtsZ

Weart, Richard B.; Nakano, Shunji; Lane, Brooke E.; Zuber, Peter; Levin, Petra Anne

doi:10.1111/j.1365-2958.2005.04673.x

Cited by 88 publications

(105 citation statements)

References 55 publications

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“…Based on these results, they proposed that ClpXP may participate in cell division by modulating the equilibrium between monomeric and polymeric FtsZ via degradation of FtsZ polymers. In contrast, it has been reported that in B. subtilis ClpXP does not degrade FtsZ and that ClpX regulates FtsZ polymer dynamics by preventing FtsZ polymerization (19). Our present results mentioned above are consistent with the latter result, but contribution of FtsZ degradation (or unfolding) by ClpXP (or ClpX) to the regulation of FtsZ polymer dynamics remains to be elucidated.…”

Section: Clpx Recognizes a C-terminal Moiety And Other Parts Of Ftsz-supporting

confidence: 66%

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AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ

Sugimoto

Yamanaka

Nishikori

et al. 2010

Journal of Biological Chemistry

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Section: Clpx Recognizes a C-terminal Moiety And Other Parts Of Ftsz-supporting

confidence: 66%

“…Recently, it has been reported that in Bacillus subtilis ClpX inhibits FtsZ polymerization in vivo and in vitro in an ATP-independent manner but does not degrade it (19,20). However, molecular mechanisms of regulating FtsZ monomerpolymer dynamics are still largely unknown.…”

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confidence: 99%

AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ

Sugimoto

Yamanaka

Nishikori

et al. 2010

Journal of Biological Chemistry

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“…As ZipA and EzrA bind directly to FtsZ, they must therefore regulate FtsZ assembly at the membrane. Recently, the conserved chaperone ClpX was also found to inhibit Z-ring formation in B. subtilis 76 . Purified ClpX can inhibit FtsZ polymerization, although GTP hydrolysis is not affected, indicating that ClpX functions after the initial assembly of protofilaments.…”

Section: Other Regulators Of Z-ring Assemblymentioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

555

484

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Binary fission of many prokaryotes as well as some eukaryotic organelles depends on the FtsZ protein, which self-assembles into a membrane-associated ring structure early in the division process. FtsZ is homologous to tubulin, the building block of the microtubule cytoskeleton in eukaryotes. Recent advances in genomics and cell-imaging techniques have paved the way for the remarkable progress in our understanding of fission in bacteria and organelles.Duplication of cells occurs by the division of a mother cell into two daughter cells. This process, known as cytokinesis, provides the force to split cells and is spatially regulated to faithfully partition the genetic material. The cytoskeleton has a crucial role in cytokinesis. In animal and fungal cells, a medial ring of actin and myosin, helped by other proteins, contracts to divide the cell. Plant cells use a cell plate, and are guided by actin filaments and microtubules. Prokaryotes, which include bacteria and archaea, possess homologues of eukaryotic cytoskeletal proteins. Most prokaryotes use a tubulin homologue, a protein known as FtsZ, to divide. Eukaryotic organelles such as chloroplasts and mitochondria evolved from bacteria, and all chloroplasts and some mitochondria use FtsZ to divide.FtsZ is thought to be the first protein to localize to the site of future division in bacteria 1 , and it assembles into what is known as the Z ring (FIG. 1). In Escherichia coli, the Z ring recruits at least ten other proteins, all of which are required for the progression and completion of cytokinesis 2 , as will be discussed below. Whereas the cytokinetic apparatus in eukaryotic cells and even organelles can be observed directly in stained thin sections by transmission electron microscopy, the Z ring and its associated factors are not detectable by these methods. This is probably because the protein machinery is largely membrane bound and resides in a densely populated cytoplasmic environment. However, the development of green fluorescent protein (GFP) fusion and improved immunofluorescence techniques over the past 10 years have been crucial in allowing the first direct visualization of many cellular components and their dynamics. For example, using GFP fusions, the dynamics of the Z ring and other components of the cell-division protein machinery can now be visualized in living bacterial cells. The combination of these new cytological tools with genomics and the Competing interests statementThe author declares no competing financial interests. HHS Public Access Author Manuscript Author ManuscriptAuthor ManuscriptAuthor Manuscript already powerful genetics of several model systems have spurred rapid progress in our understanding of the molecular cell biology of bacteria and eukaryotic organelles. This review will discuss how the recent revolutions in genomics and cell biology have provided new evolutionary and mechanistic insights into how bacterial cells and organelles divide. The FtsZ family of proteins Conservation of FtsZFtsZ is a highly conserved protein ...

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“…MciZ is a 40-amino-acid (aa) peptide involved in the inhibition of FtsZ ring assembly following sporulation in B. subtilis (29). ClpX, a part of the ClpXP protease complex, inhibits FtsZ polymerization and possibly helps to maintain cytoplasmic pools of unpolymerized FtsZ subunits (5,20,25,44,50). Finally, the Min system spatially regulates cell division by preventing FtsZ assembly at the cell poles (27).…”

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confidence: 99%