Replication protein A 32 interacts through a similar binding interface with TIPIN, XPA, and UNG2

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The 32 kDa subunit of replication protein A (RPA32) is involved in various DNA repair systems such as nucleotide excision repair, base excision repair, and homologous recombination. In these processes, RPA32 interacts with different binding partners via its C-terminal domain (RPA32C; residues 172-270). It has been reported recently that RPA32C also interacts with TIPIN during the intra-S checkpoint. To determine the significance of the interaction of RPA32C with TIPIN, we have examined the interaction mode using NMR spectroscopy and an in silico modeling approach. Here, we show that TIPIN(185-218), which shares high sequence similarity with XPA(10-43) and UNG2(56-89), is less ordered in the free state and then forms a longer cc-helix upon binding to RPA32C. The binding interface between TIPIN(185-218) and RPA32C is similar to those ofXPA and UNG2, but its mode of interaction is different.The results suggest that RPA32 is an exchange point for multiple proteins involved in DNA repair, homologous recombination, and checkpoint processes and that it binds to different partners with comparable binding affinity using a single site. (C) 2010 Elsevier Ltd. All rights reserved.
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Issue Date
2010-07
Language
English
Article Type
Article
Keywords

NUCLEOTIDE EXCISION-REPAIR; CIRCULAR-DICHROISM; DNA; SUBUNIT; NMR; RPA; RECOMBINATION; RECOGNITION; REQUIREMENT; CHECKPOINT

Citation

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, v.42, no.7, pp.1210 - 1215

ISSN
1357-2725
DOI
10.1016/j.biocel.2010.04.011
URI
http://hdl.handle.net/10203/98608
Appears in Collection
CH-Journal Papers(저널논문)
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