The Role of the Unique Motifs in the Amino-Terminal Region of PKN on Its Enzymatic Activity

The yeast two-hybrid system and in vitro binding assay were carried out to characterize the interaction between the amino-terminal and carboxyl-terminal region of PKN. It was revealed that the amino-terminal region containing the regulatory domain associated with the carboxyl-terminal catalytic regi...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1996-03, Vol.220 (3), p.963-968
Main Authors: Kitagawa, Michinori, Shibata, Hideki, Toshimori, Masanao, Mukai, Hideyuki, Ono, Yoshitaka
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Cloning, Molecular
Humans
Kinetics
Leucine Zippers
Molecular Sequence Data
Peptides - chemical synthesis
Peptides - chemistry
Phosphorylation
Protein Kinase C
Protein-Serine-Threonine Kinases
Protein-Tyrosine Kinases - biosynthesis
Protein-Tyrosine Kinases - chemistry
Protein-Tyrosine Kinases - metabolism
Rats
Recombinant Fusion Proteins - biosynthesis
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Saccharomyces cerevisiae
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The yeast two-hybrid system and in vitro binding assay were carried out to characterize the interaction between the amino-terminal and carboxyl-terminal region of PKN. It was revealed that the amino-terminal region containing the regulatory domain associated with the carboxyl-terminal catalytic region. A synthetic peptide, corresponding to the amino acid residues of PKN from 39 to 53, with substitution of isoleucine 46with serine was shown to become a potent substrate for PKN, and its wild type synthetic peptide inhibited the phosphorylation by PKN. These results suggest that the amino-terminal region of PKN contains the pseudosubstrate sequence and acts as an autoinhibitory region.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0515