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M301265200v1
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Papers In Press, published online ahead of print February 24, 2003
J. Biol. Chem, 10.1074/jbc.M301265200
Submitted on February 5, 2003
Revised on February 24, 2003
Accepted on February 24, 2003

Human replication protein A: The C-terminal RPA70 and the central RPA32 domains are involved in the interactions with the 3'-end of a primer-template DNA

Pavel E. Pestryakov, Klaus Weisshart, Bernhard Schlott, Svetlana N. Khodyreva, Elisabeth Kremmer, Frank Grosse, Olga I. Lavrik, and Heinz-Peter Nasheuer

Biochemistry, Cell Cycle Control Lab., Nat. Univ. of Ireland, Galway

Corresponding Author: h.nasheuer{at}nuigalway.ie

Although the mechanical aspects of the single-stranded DNA (ssDNA)-binding activity of human replication protein A (RPA) have been extensively studied only limited information is available about its interaction with other physiologically relevant DNA structures. RPA interacts with partial DNA-duplexes that resemble DNA intermediates found in processes of DNA replication and DNA repair. Limited proteolysis of RPA showed that RPA associated with ssDNA is less protected against proteases than RPA bound to a partial duplex DNA containing a 5'-protruding tail which had the same length as the ssDNA. Modification of both the 70 kDa and 32 kDa subunits, RPA70 and RPA32, respectively, by photoaffinity labeling indicates that RPA can bind the primer-template junction of partial duplex DNAs by interacting with the 3'-end of the primer. The identification of the protein domains modified by the photoreactive 3'-end of the primer showed that domains located in the central part of the RPA32 subunit (amino acids 43-171) and the C-terminal part of the RPA70 subunit (amino acids 432-616) are involved in these interactions.


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