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PMID: 3517353 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of an Escherichia coli protein at tyrosine.

Journal of molecular biology ·Vol. 187 ·No. 2 ·1986-01-20 ·Pages 305-8

Cortay JC, Duclos B, Cozzone AJ

Abstract

The analysis of protein phosphorylation in the bacterium Escherichia coli showed that, while most phosphoproteins are modified at serine and/or threonine residues, one of them is modified exclusively at tyrosine. This particular protein which has a molecular weight of 54,500 and a pHi value of 5.6 is found associated with the membrane/ribosome fraction of the cell.

MeSH Terms
Amino Acid Sequence Autoradiography Bacterial Proteins/metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli/metabolism Isoelectric Focusing Phosphoproteins/metabolism Phosphorylation Tyrosine
Chemicals
Bacterial Proteins Phosphoproteins Tyrosine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cortay J C
Duclos B
Cozzone A J
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1986-01-20
Pages
305-8
Language
English
Region
England
NLM ID
2985088R
Subset
IM
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