Different forms of TFIIH for transcription and DNA repair: Holo-TFIIH and a nucleotide excision repairosome

Jesper Q. Svejstrup; Zhigang Wang; William J. Feave; Xiahua Wu; David A. Bushnell; Thomas F. Donahue; Errol C. Friedberg; Roger D. Kornberg

doi:10.1016/0092-8674(95)90447-6

Different forms of TFIIH for transcription and DNA repair: Holo-TFIIH and a nucleotide excision repairosome

Jesper Q. Svejstrup, Zhigang Wang, William J. Feave, Xiahua Wu, David A. Bushnell, Thomas F. Donahue, Errol C. Friedberg, Roger D. Kornberg

Toxicology and Cancer Biology

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

248 Scopus citations

Abstract

Yeast TFIIH that is active in transcription can be dissociated into three components: a 5-subunit core, the SSL2 gene product, and a complex of 47 kDa, 45 kDa, and 33 kDa polypeptides that possesses protein kinase activity directed towards the C-terminal repeat domain of RNA polymerase II. These three components can reconstitute fully functional TFIIH, and all three are required for transcription in vitro. By contrast, TFIIH that is highly active in nucleotide excision repair (NER) lacks the kinase complex and instead contains the products of all other genes known to be required for NER in yeast: RAD1, RAD2, RAD4, RAD10, and RAD14. This repairosome is not active in reconstituted transcription in vitro and is significantly more active than any of the constituent polypeptides in correcting defective repair in extracts from strains mutated in NER genes.

Original language	English
Pages (from-to)	21-28
Number of pages	8
Journal	Cell
Volume	80
Issue number	1
DOIs	https://doi.org/10.1016/0092-8674(95)90447-6
State	Published - Jan 13 1995

Bibliographical note

Funding Information:
R. D. K. is the corresponding author for this study. We thank L. Prakash for anti-RAD14 antibodies and S. Bj6rklund and J. LaPointe for purified transcription factors. J, Q. S. was supported by a fellowship from the Danish Medical Research Council. W, J. F. was supported by a Medical Research Council of Canada Studentship. This work was supported by National Institutes of Health grants GM36659 to R. D. K., GM32263 to T. F. D., and CA12428 to E. C. F.

Funding

R. D. K. is the corresponding author for this study. We thank L. Prakash for anti-RAD14 antibodies and S. Bj6rklund and J. LaPointe for purified transcription factors. J, Q. S. was supported by a fellowship from the Danish Medical Research Council. W, J. F. was supported by a Medical Research Council of Canada Studentship. This work was supported by National Institutes of Health grants GM36659 to R. D. K., GM32263 to T. F. D., and CA12428 to E. C. F.

Funders	Funder number
National Institutes of Health (NIH)	GM36659, CA12428
National Institute of General Medical Sciences	R01GM032263
Sundhed og Sygdom, Det Frie Forskningsråd
Medical Research Council Canada

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/0092-8674(95)90447-6

Cite this

@article{1efe7e4ab698422c9459fc39c63475b8,

title = "Different forms of TFIIH for transcription and DNA repair: Holo-TFIIH and a nucleotide excision repairosome",

abstract = "Yeast TFIIH that is active in transcription can be dissociated into three components: a 5-subunit core, the SSL2 gene product, and a complex of 47 kDa, 45 kDa, and 33 kDa polypeptides that possesses protein kinase activity directed towards the C-terminal repeat domain of RNA polymerase II. These three components can reconstitute fully functional TFIIH, and all three are required for transcription in vitro. By contrast, TFIIH that is highly active in nucleotide excision repair (NER) lacks the kinase complex and instead contains the products of all other genes known to be required for NER in yeast: RAD1, RAD2, RAD4, RAD10, and RAD14. This repairosome is not active in reconstituted transcription in vitro and is significantly more active than any of the constituent polypeptides in correcting defective repair in extracts from strains mutated in NER genes.",

author = "Svejstrup, {Jesper Q.} and Zhigang Wang and Feave, {William J.} and Xiahua Wu and Bushnell, {David A.} and Donahue, {Thomas F.} and Friedberg, {Errol C.} and Kornberg, {Roger D.}",

note = "Funding Information: R. D. K. is the corresponding author for this study. We thank L. Prakash for anti-RAD14 antibodies and S. Bj6rklund and J. LaPointe for purified transcription factors. J, Q. S. was supported by a fellowship from the Danish Medical Research Council. W, J. F. was supported by a Medical Research Council of Canada Studentship. This work was supported by National Institutes of Health grants GM36659 to R. D. K., GM32263 to T. F. D., and CA12428 to E. C. F.",

year = "1995",

month = jan,

day = "13",

doi = "10.1016/0092-8674(95)90447-6",

language = "English",

volume = "80",

pages = "21--28",

number = "1",

}

TY - JOUR

T1 - Different forms of TFIIH for transcription and DNA repair

T2 - Holo-TFIIH and a nucleotide excision repairosome

AU - Svejstrup, Jesper Q.

AU - Wang, Zhigang

AU - Feave, William J.

AU - Wu, Xiahua

AU - Bushnell, David A.

AU - Donahue, Thomas F.

AU - Friedberg, Errol C.

AU - Kornberg, Roger D.

N1 - Funding Information: R. D. K. is the corresponding author for this study. We thank L. Prakash for anti-RAD14 antibodies and S. Bj6rklund and J. LaPointe for purified transcription factors. J, Q. S. was supported by a fellowship from the Danish Medical Research Council. W, J. F. was supported by a Medical Research Council of Canada Studentship. This work was supported by National Institutes of Health grants GM36659 to R. D. K., GM32263 to T. F. D., and CA12428 to E. C. F.

PY - 1995/1/13

Y1 - 1995/1/13

N2 - Yeast TFIIH that is active in transcription can be dissociated into three components: a 5-subunit core, the SSL2 gene product, and a complex of 47 kDa, 45 kDa, and 33 kDa polypeptides that possesses protein kinase activity directed towards the C-terminal repeat domain of RNA polymerase II. These three components can reconstitute fully functional TFIIH, and all three are required for transcription in vitro. By contrast, TFIIH that is highly active in nucleotide excision repair (NER) lacks the kinase complex and instead contains the products of all other genes known to be required for NER in yeast: RAD1, RAD2, RAD4, RAD10, and RAD14. This repairosome is not active in reconstituted transcription in vitro and is significantly more active than any of the constituent polypeptides in correcting defective repair in extracts from strains mutated in NER genes.

AB - Yeast TFIIH that is active in transcription can be dissociated into three components: a 5-subunit core, the SSL2 gene product, and a complex of 47 kDa, 45 kDa, and 33 kDa polypeptides that possesses protein kinase activity directed towards the C-terminal repeat domain of RNA polymerase II. These three components can reconstitute fully functional TFIIH, and all three are required for transcription in vitro. By contrast, TFIIH that is highly active in nucleotide excision repair (NER) lacks the kinase complex and instead contains the products of all other genes known to be required for NER in yeast: RAD1, RAD2, RAD4, RAD10, and RAD14. This repairosome is not active in reconstituted transcription in vitro and is significantly more active than any of the constituent polypeptides in correcting defective repair in extracts from strains mutated in NER genes.

UR - http://www.scopus.com/inward/record.url?scp=0028885363&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028885363&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(95)90447-6

DO - 10.1016/0092-8674(95)90447-6

M3 - Article

C2 - 7813015

AN - SCOPUS:0028885363

SN - 0092-8674

VL - 80

SP - 21

EP - 28

JO - Cell

JF - Cell

IS - 1

ER -

Different forms of TFIIH for transcription and DNA repair: Holo-TFIIH and a nucleotide excision repairosome

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this