Physical and Functional Interactions of Caenorhabditis elegans WRN-1 Helicase with RPA-1

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The Caenorhabditis elegans Werner syndrome protein, WRN-1, a member of the RecQ helicase family, has a 3'-5' DNA helicase activity. Worms with defective wrn-1 exhibit premature aging phenotypes and an increased level of genome instability. In response to DNA damage, WRN-1 participates in the initial stages of checkpoint activation in concert with C. elegans replication protein A (RPA-1). WRN-1 helicase is stimulated by RPA-1 on long DNA duplex substrates. However, the mechanism by which RPA-1 stimulates DNA unwinding and the function of the WRN-1-RPA-1 interaction are not clearly understood. We have found that WRN-1 physically interacts with two RPA-1 subunits, CeRPA73 and CeRPA32; however, full-length WRN-1 helicase activity is stimulated by only the CeRPA73 subunit, while the WRN-1(162-1056) fragment that harbors the helicase activity requires both the CeRPA73 and CeRPA32 subunits for the stimulation. We also found that the CeRPA73(1-464) fragment can stimulate WRN-1 helicase activity and that residues 335-464 of CeRPA73 are important for physical interaction with WRN-1. Because CeRPA73 and the CeRPA73(1-464) fragment are able to bind single-stranded DNA (ssDNA), the stimulation of WRN-1 helicase by RPA-1 is most likely due to the ssDNA binding activity of CeRPA73 and the direct interaction of WRN-1 and CeRPA73.
Publisher
AMER CHEMICAL SOC
Issue Date
2012-02
Language
English
Article Type
Article
Keywords

WERNER-SYNDROME PROTEIN; DOUBLE-STRAND BREAKS; MEDIATED DNA-DAMAGE; BLOOMS-SYNDROME PROTEIN; SYNDROME GENE-PRODUCT; RECQ HELICASES; UNWINDING ACTIVITY; REPLICATION FORKS; ESCHERICHIA-COLI; MAMMALIAN-CELLS

Citation

BIOCHEMISTRY, v.51, no.7, pp.1336 - 1345

ISSN
0006-2960
DOI
10.1021/bi200791p
URI
http://hdl.handle.net/10203/98025
Appears in Collection
BS-Journal Papers(저널논문)
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