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J Biol Chem, Vol. 274, Issue 35, 24485-24489, August 27, 1999
From the Department of Chemistry, The Pennsylvania State
University, University Park, Pennsylvania 16802
The location of the interaction of the COOH
terminus of the bacteriophage T4 DNA polymerase with its trimeric,
circular sliding clamp has been established. A peptide corresponding to
the COOH terminus of the DNA polymerase was labeled with a fluorophore and fluorescence spectroscopy used to show that it forms a specific complex with the sliding clamp by virtue of its low
KD value (7.1 ± 1.0 µM). The
same peptide was labeled with a photoaffinity probe and cross-linked to
the sliding clamp. Mass spectrometry of tryptic digests determined the
sole linkage point to be Ala-159 on the sliding clamp, an amino acid
that lies on the subunit interface. These results demonstrate that the
COOH terminus of the DNA polymerase is inserted into the subunit
interface of its sliding clamp, thereby conferring processivity to the
DNA polymerase.
The Carboxyl Terminus of the Bacteriophage T4 DNA Polymerase
Contacts Its Sliding Clamp at the Subunit Interface
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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