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

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

30 Citations (Scopus)

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

@article{c9bcbb992e7d4635a8f43a5625333dcd,

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",

language = "English",

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journal = "Mutation Research-DNA Repair",

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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.

KW - 120 kDa subunit

KW - ERCC1 protein complex

KW - Immunoprecipitation

KW - Nucleotide excision repair

KW - Purification

UR - https://www.scopus.com/pages/publications/0029011147

U2 - 10.1016/0921-8777(95)00009-9

DO - 10.1016/0921-8777(95)00009-9

M3 - Article

C2 - 7596355

AN - SCOPUS:0029011147

SN - 0921-8777

VL - 337

SP - 25

EP - 39

JO - Mutation Research-DNA Repair

JF - Mutation Research-DNA Repair

IS - 1

ER -

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

Abstract

Keywords

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