Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein

Akira Nagai; Masafumi Saijo; Isao Kuraoka; Toshiro Matsuda; Naohiko Kodo; Yoshimichi Nakatsu; Takashi Mimaki; Makoio Mino; Maureen Biggerstaff; Richard D. Wood; Anneke Sijbers; Jan H.J. Hoeijmakers; Kiyoji Tanaka

doi:10.1006/bbrc.1995.1905

Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein

Akira Nagai, Masafumi Saijo, Isao Kuraoka, Toshiro Matsuda, Naohiko Kodo, Yoshimichi Nakatsu, Takashi Mimaki, Makoio Mino, Maureen Biggerstaff, Richard D. Wood, Anneke Sijbers, Jan H.J. Hoeijmakers, Kiyoji Tanaka

Research output: Contribution to journal › Article › peer-review

55 Citations (Scopus)

Abstract

The human XPA and ERCC1 proteins, which are involved in early steps of nucleotide excision repair of DNA, specifically interacted in an in vitro binding assay and a yeast two-hybrid assay. A stretch of consecutive glutamic acid residues in XPA was needed for binding to ERCC1. Binding of XPA to damaged DNA was markedly increased by the interaction of the XPA and ERCC1 proteins. ERCC1 did not enhance binding to DNA when a truncated XPA protein, MF122, was used in place of the XPA protein. MF122 retains damaged DNA binding activity but lacks the region for protein-protein interaction including the E-cluster region. These results suggest that the XPA/ERCC1 interaction may participate in damage-recognition as well as in incision at the 5′ site of damage during nucleotide excision repair.

Original language	English
Pages (from-to)	960-966
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	211
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1995.1905
Publication status	Published - 26 Jun 1995
Externally published	Yes

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Nagai, A., Saijo, M., Kuraoka, I., Matsuda, T., Kodo, N., Nakatsu, Y., Mimaki, T., Mino, M., Biggerstaff, M., Wood, R. D., Sijbers, A., Hoeijmakers, J. H. J., & Tanaka, K. (1995). Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein. Biochemical and Biophysical Research Communications, 211(3), 960-966. https://doi.org/10.1006/bbrc.1995.1905

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title = "Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein",

abstract = "The human XPA and ERCC1 proteins, which are involved in early steps of nucleotide excision repair of DNA, specifically interacted in an in vitro binding assay and a yeast two-hybrid assay. A stretch of consecutive glutamic acid residues in XPA was needed for binding to ERCC1. Binding of XPA to damaged DNA was markedly increased by the interaction of the XPA and ERCC1 proteins. ERCC1 did not enhance binding to DNA when a truncated XPA protein, MF122, was used in place of the XPA protein. MF122 retains damaged DNA binding activity but lacks the region for protein-protein interaction including the E-cluster region. These results suggest that the XPA/ERCC1 interaction may participate in damage-recognition as well as in incision at the 5′ site of damage during nucleotide excision repair.",

author = "Akira Nagai and Masafumi Saijo and Isao Kuraoka and Toshiro Matsuda and Naohiko Kodo and Yoshimichi Nakatsu and Takashi Mimaki and Makoio Mino and Maureen Biggerstaff and Wood, {Richard D.} and Anneke Sijbers and Hoeijmakers, {Jan H.J.} and Kiyoji Tanaka",

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Nagai, A, Saijo, M, Kuraoka, I, Matsuda, T, Kodo, N, Nakatsu, Y, Mimaki, T, Mino, M, Biggerstaff, M, Wood, RD, Sijbers, A, Hoeijmakers, JHJ & Tanaka, K 1995, 'Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein', Biochemical and Biophysical Research Communications, vol. 211, no. 3, pp. 960-966. https://doi.org/10.1006/bbrc.1995.1905

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T1 - Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein

AU - Nagai, Akira

AU - Saijo, Masafumi

AU - Kuraoka, Isao

AU - Matsuda, Toshiro

AU - Kodo, Naohiko

AU - Nakatsu, Yoshimichi

AU - Mimaki, Takashi

AU - Mino, Makoio

AU - Biggerstaff, Maureen

AU - Wood, Richard D.

AU - Sijbers, Anneke

AU - Hoeijmakers, Jan H.J.

AU - Tanaka, Kiyoji

PY - 1995/6/26

Y1 - 1995/6/26

N2 - The human XPA and ERCC1 proteins, which are involved in early steps of nucleotide excision repair of DNA, specifically interacted in an in vitro binding assay and a yeast two-hybrid assay. A stretch of consecutive glutamic acid residues in XPA was needed for binding to ERCC1. Binding of XPA to damaged DNA was markedly increased by the interaction of the XPA and ERCC1 proteins. ERCC1 did not enhance binding to DNA when a truncated XPA protein, MF122, was used in place of the XPA protein. MF122 retains damaged DNA binding activity but lacks the region for protein-protein interaction including the E-cluster region. These results suggest that the XPA/ERCC1 interaction may participate in damage-recognition as well as in incision at the 5′ site of damage during nucleotide excision repair.

AB - The human XPA and ERCC1 proteins, which are involved in early steps of nucleotide excision repair of DNA, specifically interacted in an in vitro binding assay and a yeast two-hybrid assay. A stretch of consecutive glutamic acid residues in XPA was needed for binding to ERCC1. Binding of XPA to damaged DNA was markedly increased by the interaction of the XPA and ERCC1 proteins. ERCC1 did not enhance binding to DNA when a truncated XPA protein, MF122, was used in place of the XPA protein. MF122 retains damaged DNA binding activity but lacks the region for protein-protein interaction including the E-cluster region. These results suggest that the XPA/ERCC1 interaction may participate in damage-recognition as well as in incision at the 5′ site of damage during nucleotide excision repair.

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U2 - 10.1006/bbrc.1995.1905

DO - 10.1006/bbrc.1995.1905

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AN - SCOPUS:0029061081

SN - 0006-291X

VL - 211

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

Enhancement of damage-specific dna binding of xpa by interaction with the ERCC1 DNA repair protein

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