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A more recent version of this article appeared on June 29, 2001
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M100783200v1
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Papers In Press, published online ahead of print April 17, 2001
J. Biol. Chem, 10.1074/jbc.M100783200
Submitted on January 29, 2001
Revised on April 16, 2001
Accepted on April 16, 2001

Identification and mapping of protein-protein interactions between gp32 and gp59 by crosslinking

Faoud T. Ishmael, Stephen C. Alley, and Stephen J. Benkovic

Department of Chemistry, Pennsylvania State University, University Park, PA 16802

Corresponding Author: sjb1{at}psu.edu

The bacteriophage T4 59 protein (gp59) plays a vital role in recombination and replication by promoting the assembly of the gene 41 helicase (gp41) onto DNA, thus enabling replication as well as strand exchange in recombination. Loading of the helicase onto gp32 (the T4 single strand binding protein) coated single-stranded DNA requires gp59 to remove gp32 and replace it with gp41. Crosslinking studies between gp32 and gp59 reveal an interaction between Cys-166 of gp32 and Cys-42 of gp59. Since Cys-166 lies in the DNA-binding core domain of gp32, this interaction may affect the association of gp32 with DNA. In the presence of gp32 or DNA, gp59 is capable of forming a multimer consisting of at least five gp59 subunits. Kinetic studies have suggested that gp59 and gp41 exist in a one to one ratio, predicting that gp59 is capable of forming a hexamer [Raney, K. D., Carver, T. E., and Benkovic, S. J. (1996) J.Biol.Chem. 271, 14074-14081]. The C-terminal A-domain of gp32 is needed for gp59 oligomer formation. Crosslinking has established that gp59 can interact with gp32-A (a truncated form of gp32 lacking the A-domain), but cannot form higher species. Both the A-domain and core domain of gp32 contact gp59 and these interactions may be essential for loading of the helicase.


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