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From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DIVL_CAUCR DIVL_CAUCR]] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. | [[http://www.uniprot.org/uniprot/DIVL_CAUCR DIVL_CAUCR]] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | One of the simplest organisms to divide asymmetrically is the bacterium Caulobacter crescentus. The DivL pseudo-histidine kinase, positioned at one cell pole, regulates cell-fate by controlling the activation of the global transcription factor CtrA via an interaction with the response regulator (RR) DivK. DivL uniquely contains a tyrosine at the histidine phosphorylation site, and can achieve these regulatory functions in vivo without kinase activity. Determination of the DivL crystal structure and biochemical analysis of wild-type and site-specific DivL mutants revealed that the DivL PAS domains regulate binding specificity for DivK approximately P over DivK, which is modulated by an allosteric intramolecular interaction between adjacent domains. We discovered that DivL's catalytic domains have been repurposed as a phosphospecific RR input sensor, thereby reversing the flow of information observed in conventional histidine kinase (HK)-RR systems and coupling a complex network of signaling proteins for cell-fate regulation. | ||
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| + | Cell fate regulation governed by a repurposed bacterial histidine kinase.,Childers WS, Xu Q, Mann TH, Mathews II, Blair JA, Deacon AM, Shapiro L PLoS Biol. 2014 Oct 28;12(10):e1001979. doi: 10.1371/journal.pbio.1001979., eCollection 2014 Oct. PMID:25349992<ref>PMID:25349992</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:58, 18 March 2015
Crystal structure of a C-terminal part of tyrosine kinase (DivL) from Caulobacter crescentus CB15 at 2.50 A resolution (PSI Community Target, Shapiro)
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