Tyrosine phosphorylation of a membrane protein from Pseudomonas solanacearum.

Abstract:

:We have investigated a tyrosine kinase activity from Pseudomonas solanacearum, an economically important plant pathogen. In vitro incubation of membrane fractions with [gamma-32P]ATP and subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed an 85-kDa phosphoprotein. Phosphorylation of this protein on tyrosine residues was demonstrated by phosphoamino acid analysis of base hydrolysis products and by immunoanalysis of Western blots (immunoblots) with antiphosphotyrosine monoclonal antibody. In vitro incubation of membranes with ATP was not required for recognition by the antibody, indicating that the 85-kDa protein is phosphorylated in vivo. These results demonstrate that membranes from P. solanacearum exhibit a tyrosine kinase activity toward an endogenous membrane protein. This bacterium provides an opportunity to study the structure and function of a prokaryotic tyrosine kinase.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Atkinson M,Allen C,Sequeira L

doi

10.1128/jb.174.13.4356-4360.1992

keywords:

subject

Has Abstract

pub_date

1992-07-01 00:00:00

pages

4356-60

issue

13

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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