Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

A. J. van Vuuren; E. Appeldoorn; H. Odijk; S. Humbert; V. Moncollin; A. P.M. Eker; N. G.J. Jaspers; J. M. Egly; J. H.J. Hoeijmakers

doi:10.1016/0921-8777(95)00009-9

Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

A. J. van Vuuren, E. Appeldoorn, H. Odijk, S. Humbert, V. Moncollin, A. P.M. Eker, N. G.J. Jaspers, J. M. Egly, J. H.J. Hoeijmakers

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Abstract

The nucleotide excision repair (NER) protein ERCC1 is part of a functional complex, which harbors in addition the repair correctig activities of ERCC4, ERCC11 and human XPF. ERCC1 is not associated with a defect in any of the known human NER disorders: xeroderma pigmentosum, Cockayne's syndrome or trichothiodystrophy. Here we report the partial purification and characterization of the ERCC1 complex. Immunoprecipitation studies tentatively identified a subunit in the complex with an apparent MW of ∼ 120 kDa. The complex has affinity for DNA, but no clear preference for ss, ds or UV-damaged DNA substrates. The size of the entire complex determined by non-denaturing gradient gels (∼ 280 kDa) is considerably larger than previously found using size separation on glycerol gradients (∼ 120 kDa). Stable associations of the ERCC1 complex with other known repair factors (XPA, XPC, XPG and TFIIH complex) could not be detected.

Original language	English
Pages (from-to)	25-39
Number of pages	15
Journal	Mutation Research-DNA Repair
Volume	337
Issue number	1
DOIs	https://doi.org/10.1016/0921-8777(95)00009-9
Publication status	Published - Jul 1995
Externally published	Yes

Keywords

120 kDa subunit
ERCC1 protein complex
Immunoprecipitation
Nucleotide excision repair
Purification

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10.1016/0921-8777(95)00009-9

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van Vuuren, A. J., Appeldoorn, E., Odijk, H., Humbert, S., Moncollin, V., Eker, A. P. M., Jaspers, N. G. J., Egly, J. M., & Hoeijmakers, J. H. J. (1995). Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities. Mutation Research-DNA Repair, 337(1), 25-39. https://doi.org/10.1016/0921-8777(95)00009-9

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title = "Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities",

abstract = "The nucleotide excision repair (NER) protein ERCC1 is part of a functional complex, which harbors in addition the repair correctig activities of ERCC4, ERCC11 and human XPF. ERCC1 is not associated with a defect in any of the known human NER disorders: xeroderma pigmentosum, Cockayne's syndrome or trichothiodystrophy. Here we report the partial purification and characterization of the ERCC1 complex. Immunoprecipitation studies tentatively identified a subunit in the complex with an apparent MW of ∼ 120 kDa. The complex has affinity for DNA, but no clear preference for ss, ds or UV-damaged DNA substrates. The size of the entire complex determined by non-denaturing gradient gels (∼ 280 kDa) is considerably larger than previously found using size separation on glycerol gradients (∼ 120 kDa). Stable associations of the ERCC1 complex with other known repair factors (XPA, XPC, XPG and TFIIH complex) could not be detected.",

keywords = "120 kDa subunit, ERCC1 protein complex, Immunoprecipitation, Nucleotide excision repair, Purification",

author = "{van Vuuren}, {A. J.} and E. Appeldoorn and H. Odijk and S. Humbert and V. Moncollin and Eker, {A. P.M.} and Jaspers, {N. G.J.} and Egly, {J. M.} and Hoeijmakers, {J. H.J.}",

note = "Funding Information: We are gratefult o W.L. de Laat for help with someo f the experimentst,o A. Raamsf or preparing cell-free extracts,a nd to M. Kuit for photography.T his work was supportedi n part by grants from the NetherlandsF oundation for Chemical Research (SON), Medical Sciences( GMW, 900-501-11 3), Commissiono f European Community (Contract No. BJ6-141-NL), the INSERM, the CNRS, the Minister-ed e la Recherchee t de l{\textquoteright}En-seignementS uperieur, and the Associationp our la Recherches ur le Cancer.",

year = "1995",

month = jul,

doi = "10.1016/0921-8777(95)00009-9",

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T1 - Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

AU - van Vuuren, A. J.

AU - Appeldoorn, E.

AU - Odijk, H.

AU - Humbert, S.

AU - Moncollin, V.

AU - Eker, A. P.M.

AU - Jaspers, N. G.J.

AU - Egly, J. M.

AU - Hoeijmakers, J. H.J.

N1 - Funding Information: We are gratefult o W.L. de Laat for help with someo f the experimentst,o A. Raamsf or preparing cell-free extracts,a nd to M. Kuit for photography.T his work was supportedi n part by grants from the NetherlandsF oundation for Chemical Research (SON), Medical Sciences( GMW, 900-501-11 3), Commissiono f European Community (Contract No. BJ6-141-NL), the INSERM, the CNRS, the Minister-ed e la Recherchee t de l’En-seignementS uperieur, and the Associationp our la Recherches ur le Cancer.

PY - 1995/7

Y1 - 1995/7

N2 - The nucleotide excision repair (NER) protein ERCC1 is part of a functional complex, which harbors in addition the repair correctig activities of ERCC4, ERCC11 and human XPF. ERCC1 is not associated with a defect in any of the known human NER disorders: xeroderma pigmentosum, Cockayne's syndrome or trichothiodystrophy. Here we report the partial purification and characterization of the ERCC1 complex. Immunoprecipitation studies tentatively identified a subunit in the complex with an apparent MW of ∼ 120 kDa. The complex has affinity for DNA, but no clear preference for ss, ds or UV-damaged DNA substrates. The size of the entire complex determined by non-denaturing gradient gels (∼ 280 kDa) is considerably larger than previously found using size separation on glycerol gradients (∼ 120 kDa). Stable associations of the ERCC1 complex with other known repair factors (XPA, XPC, XPG and TFIIH complex) could not be detected.

AB - The nucleotide excision repair (NER) protein ERCC1 is part of a functional complex, which harbors in addition the repair correctig activities of ERCC4, ERCC11 and human XPF. ERCC1 is not associated with a defect in any of the known human NER disorders: xeroderma pigmentosum, Cockayne's syndrome or trichothiodystrophy. Here we report the partial purification and characterization of the ERCC1 complex. Immunoprecipitation studies tentatively identified a subunit in the complex with an apparent MW of ∼ 120 kDa. The complex has affinity for DNA, but no clear preference for ss, ds or UV-damaged DNA substrates. The size of the entire complex determined by non-denaturing gradient gels (∼ 280 kDa) is considerably larger than previously found using size separation on glycerol gradients (∼ 120 kDa). Stable associations of the ERCC1 complex with other known repair factors (XPA, XPC, XPG and TFIIH complex) could not be detected.

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KW - ERCC1 protein complex

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KW - Nucleotide excision repair

KW - Purification

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ER -

Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

Abstract

Keywords

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