Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. / Feaver, William J.; Svejstrup, Jesper Q.; Henry, N. Lynn; Kornberg, Roger D.

In: Cell, Vol. 79, No. 6, 16.12.1994, p. 1103-1109.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Feaver, WJ, Svejstrup, JQ, Henry, NL & Kornberg, RD 1994, 'Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK', Cell, vol. 79, no. 6, pp. 1103-1109. https://doi.org/10.1016/0092-8674(94)90040-X

APA

Feaver, W. J., Svejstrup, J. Q., Henry, N. L., & Kornberg, R. D. (1994). Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell, 79(6), 1103-1109. https://doi.org/10.1016/0092-8674(94)90040-X

Vancouver

Feaver WJ, Svejstrup JQ, Henry NL, Kornberg RD. Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell. 1994 Dec 16;79(6):1103-1109. https://doi.org/10.1016/0092-8674(94)90040-X

Author

Feaver, William J. ; Svejstrup, Jesper Q. ; Henry, N. Lynn ; Kornberg, Roger D. / Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. In: Cell. 1994 ; Vol. 79, No. 6. pp. 1103-1109.

Bibtex

@article{f6f27a946dc84c20a313b90191205f64,
title = "Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK",
abstract = "KIN28, a member of the p34 cdc2 CDC28 family of protein kinases, is identified as a subunit of yeast RNA polymerase transcription factor IIH (TFIIH) on the basis of sequence determination, immunological reactivity, and copurification. KIN28 is, moreover, one of three subunits of TFIIK, a subassembly of TFIIH with protein kinase activity directed toward the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II. Itself a phosphoprotein, KIN28 interacts specifically with the two largest subunits of RNA polymerase II. Previous work of others points to two further associations: KIN28 interacts in vivo with the cyclin CCL1, and KIN28 and CCL1 are homologous to human MO15 and cyclin H, which form the cyclin-dependent kinaseactivating kinase (CAK). We show that human CAK possesses the CTD kinase activity characteristic of TFIIH.",
author = "Feaver, {William J.} and Svejstrup, {Jesper Q.} and Henry, {N. Lynn} and Kornberg, {Roger D.}",
year = "1994",
month = dec,
day = "16",
doi = "10.1016/0092-8674(94)90040-X",
language = "English",
volume = "79",
pages = "1103--1109",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK

AU - Feaver, William J.

AU - Svejstrup, Jesper Q.

AU - Henry, N. Lynn

AU - Kornberg, Roger D.

PY - 1994/12/16

Y1 - 1994/12/16

N2 - KIN28, a member of the p34 cdc2 CDC28 family of protein kinases, is identified as a subunit of yeast RNA polymerase transcription factor IIH (TFIIH) on the basis of sequence determination, immunological reactivity, and copurification. KIN28 is, moreover, one of three subunits of TFIIK, a subassembly of TFIIH with protein kinase activity directed toward the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II. Itself a phosphoprotein, KIN28 interacts specifically with the two largest subunits of RNA polymerase II. Previous work of others points to two further associations: KIN28 interacts in vivo with the cyclin CCL1, and KIN28 and CCL1 are homologous to human MO15 and cyclin H, which form the cyclin-dependent kinaseactivating kinase (CAK). We show that human CAK possesses the CTD kinase activity characteristic of TFIIH.

AB - KIN28, a member of the p34 cdc2 CDC28 family of protein kinases, is identified as a subunit of yeast RNA polymerase transcription factor IIH (TFIIH) on the basis of sequence determination, immunological reactivity, and copurification. KIN28 is, moreover, one of three subunits of TFIIK, a subassembly of TFIIH with protein kinase activity directed toward the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II. Itself a phosphoprotein, KIN28 interacts specifically with the two largest subunits of RNA polymerase II. Previous work of others points to two further associations: KIN28 interacts in vivo with the cyclin CCL1, and KIN28 and CCL1 are homologous to human MO15 and cyclin H, which form the cyclin-dependent kinaseactivating kinase (CAK). We show that human CAK possesses the CTD kinase activity characteristic of TFIIH.

UR - http://www.scopus.com/inward/record.url?scp=0028590113&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(94)90040-X

DO - 10.1016/0092-8674(94)90040-X

M3 - Journal article

C2 - 8001136

AN - SCOPUS:0028590113

VL - 79

SP - 1103

EP - 1109

JO - Cell

JF - Cell

SN - 0092-8674

IS - 6

ER -

ID: 331042827