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Science 24 January 1986:
Vol. 231. no. 4736, pp. 390 - 393
DOI: 10.1126/science.2417318
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Articles

Science, Vol 231, Issue 4736, 390-393
Copyright © 1986 by American Association for the Advancement of Science

articles

Protein-tyrosine kinase activity in Saccharomyces cerevisiae

G Schieven, J Thorner, and GS Martin

Saccharomyces cerevisiae was examined for tyrosine kinase activity in vitro because this organism offers molecular and genetic approaches for analyzing the role of tyrosine phosphorylation in cellular growth control that are unavailable in higher eukaryotes. Yeast extracts phosphorylated a random copolymer (glutamic acid:tyrosine, 80:20) at tyrosine in a reaction that was linear with respect to time and protein concentration. In the absence of added copolymer, phosphotyrosine was 0.1 percent of the total phosphoamino acids labeled with [gamma-32P]adenosine triphosphate in endogenous yeast proteins. However, specific activities of these reactions were low (approximately 1 percent of those in extracts of chick embryo fibroblasts). Lack of significant incorporation of label from [alpha-32P]adenosine triphosphate into the copolymer or endogenous yeast proteins demonstrated that nucleotide interconversion, adenylylation, and subsequent hydrolysis could not account for the generation of phosphotyrosine observed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
From the Cover: Evolution of the phospho-tyrosine signaling machinery in premetazoan lineages.
D. Pincus, I. Letunic, P. Bork, and W. A. Lim (2008)
PNAS 105, 9680-9684
   Abstract »    Full Text »    PDF »
Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.
Y. Xu, M. A. Singer, and S. Lindquist (1999)
PNAS 96, 109-114
   Abstract »    Full Text »    PDF »


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