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PMID: 6129242 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Covalent phosphorylation of the Mg2+-dependent ATPase of yeast plasma membranes.

The Journal of biological chemistry ·Vol. 257 ·No. 24 ·1982-12-25 ·Pages 14579-81

McDonough JP, Mahler HP

Abstract

Phosphorylation by [gamma-32P]ATP of proteins associated with the plasma membrane of Saccharomyces cerevisiae has been studied both in vivo and in vitro. Although at least nine proteins are labeled in vivo, there is only one major protein labeled in vitro. This species with an apparent molecular weight of 114,000 has been identified as the plasma membrane Mg2+-ATPase. Phosphorylation of this enzyme occurs exclusively on serine residues. This is the first report that the proton-translocating ATPase of fungal plasma membranes is subject to phosphorylation by a protein kinase.

MeSH Terms
Adenosine Triphosphatases/metabolism Ca(2+) Mg(2+)-ATPase Cell Membrane/enzymology Kinetics Membrane Proteins/metabolism Molecular Weight Phosphorus Radioisotopes Phosphorylation Saccharomyces cerevisiae/enzymology
Chemicals
Membrane Proteins Phosphorus Radioisotopes Adenosine Triphosphatases Ca(2+) Mg(2+)-ATPase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
McDonough J P
Mahler H P
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1982-12-25
Pages
14579-81
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
PHS HHS · KO6 05060 · United States
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