Levin, L. R., Kuret, J., Johnson, K. E., Powers, S., Cameron, S., Michaeli, T., Wigler, M. H., Zoller, M. J. (April 1988) A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation. Science, 240 (4848). pp. 68-70.
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: | 1 April 1988 |
Date Deposited: | 12 Apr 2012 15:51 |
Last Modified: | 18 Nov 2016 17:16 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/26215 |
Actions (login required)
Administrator's edit/view item |