A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation

Levin, L. R., Kuret, J., Johnson, K. E., Powers, S., Cameron, S., Michaeli, T., Wigler, M. H., Zoller, M. J. (1988) A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation. Science, 240 (4848). pp. 68-70.

URL: https://www.ncbi.nlm.nih.gov/pubmed/2832943
DOI: 10.1126/science.2832943

Abstract

A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contants a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.

Item Type: Paper
Subjects: organism description > yeast > Saccharomyces
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > mutations
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
CSHL Authors:
Communities: CSHL labs > Wigler lab
CSHL labs > Powers lab
Depositing User: CSHL Librarian
Date Deposited: 12 Apr 2012 15:51
Last Modified: 18 Nov 2016 17:16
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26215

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