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PMID: 7011390 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit.

Biochimica et biophysica acta ·Vol. 633 ·No. 3 ·1980-12-15 ·Pages 376-85

Kudlicki W, Szyszka R, Paleń E, Gasior E

Abstract

Two distinct, cyclic AMP-independent protein kinase (ATP : protein photransferase, EC 2.7.1.37) from yeast have been isolated and highly purified. The first of the enzymes, protein kinase 1 A, phosphorylates casein and phosvitin, and its cellular protein substrate is unknown. The second enzyme, protein kinase 1 B, phosphorylates two strongly acidic proteins, L44 and L45, of the 60 S ribosomal subunit.

MeSH Terms

Adenosine Triphosphate/metabolism Kinetics Magnesium/pharmacology Phosphorylation Protein Kinases/classification,metabolism Ribosomal Protein L3 Ribosomal Proteins/metabolism Ribosomes/metabolism Saccharomyces cerevisiae/metabolism Substrate Specificity

Chemicals

Ribosomal Protein L3 Ribosomal Proteins ribosomal protein L2 Adenosine Triphosphate Protein Kinases Magnesium

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Kudlicki W

Szyszka R

Paleń E

Gasior E

Article Info

Journal

Biochimica et biophysica acta

Abbr.

Biochim Biophys Acta

ISSN

0006-3002

DOI

10.1016/0304-4165(80)90196-8

Published

1980-12-15

Pages

376-85

Language

English

Region

Netherlands

NLM ID

0217513

Subset

External Links

PubMed source DOI: 10.1016/0304-4165(80)90196-8

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Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit.

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