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PMID: 9023231 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Role of His243 in the phosphatase activity of EnvZ in Escherichia coli.

Journal of bacteriology ·Vol. 179 ·No. 4 ·1997-02-00 ·Pages 1413-6

Skarphol K, Waukau J, Forst SA

Abstract

EnvZ undergoes autophosphorylation at His243 and subsequently transfers the phosphate group to OmpR. EnvZ also possesses an OmpR-phosphate phosphatase activity. We examined the role of His243 in the phosphatase function by replacing His with either Val, Tyr, Ser, Asp, or Asn. EnvZH243V and EnvZH243Y were both shown to possess phosphatase activity in vitro. In addition, the mutant proteins were able to reduce the high level of OmpR-phosphate present in the envZ473 strain. These results indicate that His243 of EnvZ is not essential for stimulating the dephosphorylation of OmpR-phosphate.

MeSH Terms
Bacterial Outer Membrane Proteins/chemistry,isolation & purification,metabolism Escherichia coli/enzymology Escherichia coli Proteins Histidine/metabolism Multienzyme Complexes Mutagenesis Mutation Phosphoprotein Phosphatases/chemistry,isolation & purification,metabolism Phosphorylation
Chemicals
Bacterial Outer Membrane Proteins Escherichia coli Proteins Multienzyme Complexes Histidine envZ protein, E coli Phosphoprotein Phosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Skarphol K
Department of Biological Sciences, University of Wisconsin--Milwaukee, 53201, USA.
Waukau J
Forst S A
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.179.4.1413-1416.1997
Published
1997-02-00
Pages
1413-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC178845
Subset
IM
Grants
NIGMS NIH HHS · GM44671 · United States
External Links
PubMed source DOI: 10.1128/jb.179.4.1413-1416.1997 PMC Full Text View journal details
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