Nucleic Acids Research, Vol 24, Issue 23 4719-4724, Copyright © 1996 by Oxford University Press
M Saijo, I Kuraoka, C Masutani, F Hanaoka and K Tanaka
Recent studies have shown that many proteins are involved in the early
steps of nucleotide excision repair and that there are some interactions
between nucleotide excision repair proteins, suggesting that these
interactions are important in the reaction mechanism. The xeroderma
pigmentosum group A protein (XPA) was shown to bind to the replication
protein A (RPA) or the excision repair cross complementing rodent repair
deficiency group 1 protein (ERCC1), and these interactions might be
involved in the damage-recognition and/or incision steps, of nucleotide
excision repair. Here we show that the XPA regions required for the binding
to the 70 and 34 kDa subunits of RPA are located in the middle and on
N-terminal regions of XPA, respectively. These regions do not overlap with
the ERCC1-binding region of XPA, and a ternary protein complex of RPA, XPA
and ERCC1 was detected in vitro. In addition, using the surface plasmon
resonance biosensor, the binding of RPA and ERCC1 to XPA was investigated.
The dissociation constants (KD) of RPA and ERCC1 with XPA were 1.9 x 10(-8
)and 2.5 x 10(-7) M, respectively. Moreover, our results suggest the
sequential binding of RPA and ERCC1 to XPA.
ARTICLES
Sequential binding of DNA repair proteins RPA and ERCC1 to XPA in vitro
Division of Cellular Genetics, Institute for Molecular and Cellular Biology, Osaka University, Japan.
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