A Protein Phosphatase-1-binding Motif Identified by the Panning of a Random Peptide Display Library*
- From the Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101
Abstract
An unusually large number of regulatory or targeting proteins that bind to the catalytic subunit of protein phosphatase-1 have been recently reported. This can be explained by their possession of a common protein motif that interacts with a binding site on protein phosphatase-1. The existence of such a motif was established by the panning of a random peptide library in which peptide sequences are displayed on the Escherichia colibacterial flagellin protein for bacteria that bound to protein phosphatase-1. There were 79 isolates containing 46 unique sequences with the conserved motif VXF or VXW, whereX was most frequently His or Arg. In addition, this sequence was commonly preceded by 2–5 basic residues and followed by 1 acidic residue. This study demonstrates that binding to protein phosphatase-1 can be conferred to a protein by the presentation of a peptide motif on a surface loop. This binding motif is found in a number of protein phosphatase-1-binding proteins.
Footnotes
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↵* This work was supported by National Institutes of Health Grant DK18512.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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↵‡ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, New York Medical College, Valhalla, NY 10595. Tel.: 914-594-4057; Fax: 914-594-4058.
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↵1 The abbreviations used are: PP1, protein phosphatase-1; PAGE, polyacrylamide gel electrophoresis.
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- Received July 24, 1997.
- Revision received September 5, 1997.
