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Title: Cell fate regulation governed by a repurposed bacterial histidine kinase

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~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.
 [1] ;  [2] ;  [1] ;  [2] ;  [1] ;  [2] ;  [1] ;  [3]
  1. Stanford Univ. School of Medicine, Stanford, CA (United States)
  2. SLAC National Accelerator Laboratory, Menlo Park, CA (United States)
  3. Rutgers Univ., New Brunswick, NJ (United States)
Publication Date:
OSTI Identifier:
Grant/Contract Number:
Accepted Manuscript
Journal Name:
PLoS biology (Online)
Additional Journal Information:
Journal Name: PLoS biology (Online); Journal Volume: 12; Journal Issue: 10; Journal ID: ISSN 1545-7885
Public Library of Science
Research Org:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES phosphorylation; xylose; binding analysis; cell cycle and cell division; point mutation; crystal structure; caulobacter; histidine