4q20

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.