| pubmed-article:15948963 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15948963 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15948963 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:15948963 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:15948963 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:15948963 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15948963 | pubmed:dateCreated | 2005-6-13 | lld:pubmed |
| pubmed-article:15948963 | pubmed:abstractText | Summary Assembly of the tubulin-like cytoskeletal protein FtsZ into a ring structure establishes the location of the nascent division site in prokaryotes. Factors that modulate FtsZ assembly are essential for ensuring the precise spatial and temporal regulation of cytokinesis. We have identified ClpX, the substrate recognition subunit of the ClpXP protease, as an inhibitor of FtsZ assembly in Bacillus subtilis. Genetic data indicate that ClpX but not ClpP inhibits FtsZ-ring formation in vivo. In vitro, ClpX inhibits FtsZ assembly in a ClpP-independent manner through a mechanism that does not require ATP hydrolysis. Together our data support a model in which ClpX helps maintain the cytoplasmic pool of unassembled FtsZ that is required for the dynamic nature of the cytokinetic ring. ClpX is conserved throughout bacteria and has been shown to interact directly with FtsZ in Escherichia coli. Thus, we speculate that ClpX functions as a general regulator of FtsZ assembly and cell division in a wide variety of bacteria. | lld:pubmed |
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| pubmed-article:15948963 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15948963 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15948963 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15948963 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15948963 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15948963 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:15948963 | pubmed:author | pubmed-author:NakanoShunjiS | lld:pubmed |
| pubmed-article:15948963 | pubmed:author | pubmed-author:ZuberPeterP | lld:pubmed |
| pubmed-article:15948963 | pubmed:author | pubmed-author:WeartRichard... | lld:pubmed |
| pubmed-article:15948963 | pubmed:author | pubmed-author:LevinPetra... | lld:pubmed |
| pubmed-article:15948963 | pubmed:author | pubmed-author:LaneBrooke... | lld:pubmed |
| pubmed-article:15948963 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15948963 | pubmed:volume | 57 | lld:pubmed |
| pubmed-article:15948963 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15948963 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15948963 | pubmed:pagination | 238-49 | lld:pubmed |
| pubmed-article:15948963 | pubmed:dateRevised | 2009-9-3 | lld:pubmed |
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| pubmed-article:15948963 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15948963 | pubmed:articleTitle | The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ. | lld:pubmed |
| pubmed-article:15948963 | pubmed:affiliation | Department of Biology, Washington University, St Louis, MO 63130, USA. | lld:pubmed |
| pubmed-article:15948963 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15948963 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15948963 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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