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(Received for publication, December 7, 1994; and in revised form, January 13,
1995) We provide here a detailed characterization of two isoforms of
the protein kinase inhibitor (PKI) protein of cAMP-dependent protein
kinase that have dramatically different inhibition constants. Murine
PKI
Volume 270,
Number 13,
Issue of March 31, 1995 pp. 7227-7232
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
1 possesses a 32-fold higher K
than murine PKI
as determined by Henderson analysis.
This finding led to the investigation of C subunit
PKI
interactions involving nonconserved regions in the carboxyl and amino
termini of murine PKI and PKI1. Chimeric cDNAs coding for
amino acid sequences from both PKI isoforms were constructed and
expressed in bacteria. Surprisingly, exchanging the carboxyl-terminal
two-thirds of PKI and PKI1 has relatively little effect on
the inhibition constants of the two isoforms. Similarly, introducing
amino acid residues corresponding to a -turn region of PKI
into PKI1 fails to lower PKI1 inhibition constants. However,
introducing the amino-terminal -helical region of PKI into
PKI1 reduces the K and IC
of PKI1 to values identical with full length PKI.
Site-directed mutagenesis of specific residues within this region
implicates the presence of a tyrosine at position 7 in PKI as a
major contributor to its enhanced inhibitory potency. The results of
this study suggest that variations in C subunitPKI interactions
within an amino-terminal -helix provide a major mechanism for
altering the inhibitory properties of PKI isoforms.
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