An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae

Michael S. Kobor; Jacques Archambault; William Lester; Frank C.P. Holstege; Opher Gileadi; David B. Jansma; Ezra G. Jennings; Fiona Kouyoumdjian; Alan R. Davidson; Richard A. Young; Jack Greenblatt

doi:10.1016/S1097-2765(00)80187-2

An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae

Michael S. Kobor, Jacques Archambault, William Lester, Frank C.P. Holstege, Opher Gileadi, David B. Jansma, Ezra G. Jennings, Fiona Kouyoumdjian, Alan R. Davidson, Richard A. Young, Jack Greenblatt

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The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, ψψψ DXDX(T/V)ψψ, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.

Originele taal-2	Engels
Pagina's (van-tot)	55-62
Aantal pagina's	8
Tijdschrift	Molecular Cell
Volume	4
Nummer van het tijdschrift	1
DOI's	https://doi.org/10.1016/S1097-2765(00)80187-2
Status	Gepubliceerd - jul. 1999
Extern gepubliceerd	Ja

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10.1016/S1097-2765(00)80187-2

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Kobor, M. S., Archambault, J., Lester, W., Holstege, F. C. P., Gileadi, O., Jansma, D. B., Jennings, E. G., Kouyoumdjian, F., Davidson, A. R., Young, R. A., & Greenblatt, J. (1999). An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Molecular Cell, 4(1), 55-62. https://doi.org/10.1016/S1097-2765(00)80187-2

@article{ac2778b7c77442d09f1435c50733ddd0,

title = "An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae",

abstract = "The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, ψψψ DXDX(T/V)ψψ, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.",

author = "Kobor, {Michael S.} and Jacques Archambault and William Lester and Holstege, {Frank C.P.} and Opher Gileadi and Jansma, {David B.} and Jennings, {Ezra G.} and Fiona Kouyoumdjian and Davidson, {Alan R.} and Young, {Richard A.} and Jack Greenblatt",

note = "Funding Information: We thank Z. Moqtaderi, K. Struhl, D. Bentley, S. Orlicky, A. Edwards, P. Tran, and M. Sayre for reagents used in this study; D. Xu for advice with yeast genetics; G. Zhong for insect cell cultures; and J. Segall and J. Ingles for critical reading of the manuscript. F. C. P. H. was supported by a fellowship from the Human Frontier Science Program; E. G. J. is a predoctoral fellow of the Howard Hughes Medical Institute. This work was supported by a grant to J. G. from the National Cancer Institute of Canada with funds from the Canadian Cancer Society. J. G. is an International Research Scholar of the Howard Hughes Medical Institute.",

year = "1999",

month = jul,

doi = "10.1016/S1097-2765(00)80187-2",

language = "English",

volume = "4",

pages = "55--62",

journal = "Molecular Cell",

issn = "1097-2765",

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Kobor, MS, Archambault, J, Lester, W, Holstege, FCP, Gileadi, O, Jansma, DB, Jennings, EG, Kouyoumdjian, F, Davidson, AR, Young, RA & Greenblatt, J 1999, 'An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae', Molecular Cell, vol. 4, nr. 1, blz. 55-62. https://doi.org/10.1016/S1097-2765(00)80187-2

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T1 - An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae

AU - Kobor, Michael S.

AU - Archambault, Jacques

AU - Lester, William

AU - Holstege, Frank C.P.

AU - Gileadi, Opher

AU - Jansma, David B.

AU - Jennings, Ezra G.

AU - Kouyoumdjian, Fiona

AU - Davidson, Alan R.

AU - Young, Richard A.

AU - Greenblatt, Jack

N1 - Funding Information: We thank Z. Moqtaderi, K. Struhl, D. Bentley, S. Orlicky, A. Edwards, P. Tran, and M. Sayre for reagents used in this study; D. Xu for advice with yeast genetics; G. Zhong for insect cell cultures; and J. Segall and J. Ingles for critical reading of the manuscript. F. C. P. H. was supported by a fellowship from the Human Frontier Science Program; E. G. J. is a predoctoral fellow of the Howard Hughes Medical Institute. This work was supported by a grant to J. G. from the National Cancer Institute of Canada with funds from the Canadian Cancer Society. J. G. is an International Research Scholar of the Howard Hughes Medical Institute.

PY - 1999/7

Y1 - 1999/7

N2 - The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, ψψψ DXDX(T/V)ψψ, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.

AB - The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, ψψψ DXDX(T/V)ψψ, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.

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DO - 10.1016/S1097-2765(00)80187-2

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AN - SCOPUS:0033165865

SN - 1097-2765

VL - 4

SP - 55

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JF - Molecular Cell

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An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae

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