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Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155515
Author(s) Paul, Ralf; Jaeger, Tina; Abel, Sören; Wiederkehr, Irene; Folcher, Marc; Biondi, Emanuele G; Laub, Michael T; Jenal, Urs
Author(s) at UniBasel Jenal, Urs
Year 2008
Title Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate
Journal Cell
Volume 133
Number 3
Pages / Article-Number 452-61
Keywords Allosteric Regulation; Bacterial Proteins/genetics/*metabolism; Caulobacter crescentus/*cytology/enzymology/genetics/*metabolism; Phosphoric Monoester Hydrolases/metabolism; Phosphorylation; Phosphotransferases/metabolism; Protein Kinases/*metabolism; Signal Transduction
Abstract The two-component phosphorylation network is of critical importance for bacterial growth and physiology. Here, we address plasticity and interconnection of distinct signal transduction pathways within this network. In Caulobacter crescentus antagonistic activities of the PleC phosphatase and DivJ kinase localized at opposite cell poles control the phosphorylation state and subcellular localization of the cell fate determinator protein DivK. We show that DivK functions as an allosteric regulator that switches PleC from a phosphatase into an autokinase state and thereby mediates a cyclic di-GMP-dependent morphogenetic program. Through allosteric activation of the DivJ autokinase, DivK also stimulates its own phosphorylation and polar localization. These data suggest that DivK is the central effector of an integrated circuit that operates via spatially organized feedback loops to control asymmetry and cell fate determination in C. crescentus. Thus, single domain response regulators can facilitate crosstalk, feedback control, and long-range communication among members of the two-component network.
Publisher Cell Press
ISSN/ISBN 0092-8674
edoc-URL http://edoc.unibas.ch/dok/A5258536
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.cell.2008.02.045
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/18455986
ISI-Number WOS:000255503900016
Document type (ISI) Journal Article
 
   

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