Document Detail

Interdomain communication in the Mycobacterium tuberculosis environmental phosphatase Rv1364c.
MedLine Citation:
PMID:  19700407     Owner:  NLM     Status:  MEDLINE    
An "environmental phosphatase" controls bacterial transcriptional responses through alternative sigma factor subunits of RNA polymerase and a partner switching mechanism has been proposed to mediate phosphatase regulation. In many bacteria, the environmental phosphatase and multiple regulators are encoded in separate genes whose products form transient complexes. In contrast, in the Mycobacterium tuberculosis homolog, Rv1364c, the phosphatase is fused to two characteristic regulatory modules with sequence similarities to anti-sigma factor kinases and anti-anti-sigma factor proteins. Here we exploit this fusion to explore interactions between the phosphatase and the regulatory domains. We show quantitatively that the anti-sigma factor kinase domain activates the phosphatase domain, the kinase-phosphatase fusion protein autophosphorylates in Escherichia coli, and phosphorylation is antagonized by the phosphatase activity. Small angle x-ray scattering defines solution structures consistent with the interdomain communication observed biochemically. Taken together, these data indicate that Rv1364c provides a single chain framework to understand the structure, function, and regulation of environmental phosphatases throughout the bacterial kingdom.
Andrew E Greenstein; Michal Hammel; Alexandra Cavazos; Tom Alber
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2009-08-20
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Oct 
Date Detail:
Created Date:  2009-10-19     Completed Date:  2009-11-23     Revised Date:  2013-05-31    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  29828-35     Citation Subset:  IM    
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3220, USA.
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MeSH Terms
Mycobacterium tuberculosis / enzymology*
Phosphoric Monoester Hydrolases / chemistry*,  metabolism
Phosphorylation / physiology
Protein Structure, Tertiary / physiology
Scattering, Radiation
Structure-Activity Relationship
Grant Support
Reg. No./Substance:
EC 3.1.3.-/Phosphoric Monoester Hydrolases

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