A protein phosphatase functions to recycle RNA polymerase II

Helen Cho, Tae Kyung Kim, Helena Mancebo, William S. Lane, Osvaldo Flores, Danny Reinberg

Research output: Contribution to journalArticle

161 Citations (Scopus)

Abstract

Transcription is regulated by the state of phosphorylation of a heptapeptide repeat known as the carboxy-terminal domain (CTD) present in the largest subunit of RNA polymerase II (RNAPII). RNAPII that associates with transcription initiation complexes contains an unphosphorylated CTD, whereas the elongating polymerase has a phosphorylated CTD. Transcription factor IIH has a kinase activity specific for the CTD that is stimulated by the formation of a transcription initiation complex. Here, we report the isolation of a cDNA clone encoding a 150-kD polypeptide, which, together with RNAPII, reconstitutes a highly specific CTD phosphatase activity. Functional analysis demonstrates that the CTD phosphatase allows recycling of RNAPII. The phosphatase dephosphorylates the CTD allowing efficient incorporation of RNAPII into transcription initiation complexes, which results in increased transcription. The CTD phosphatase was found to be active in ternary elongation complexes. Moreover, the phosphatase stimulates elongation by RNAPII; however, this function is independent of its catalytic activity.

Original languageEnglish (US)
Pages (from-to)1540-1552
Number of pages13
JournalGenes and Development
Volume13
Issue number12
StatePublished - Jun 15 1999

Fingerprint

RNA Polymerase II
Phosphoprotein Phosphatases
Transcription Factor TFIIH
Recycling
Phosphoric Monoester Hydrolases
Phosphotransferases
Complementary DNA
Clone Cells
Phosphorylation
Peptides
carboxy-terminal domain phosphatase

Keywords

  • CTD phosphatase
  • Phosphorylation
  • RNA polymerase II
  • Transcription

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

Cho, H., Kim, T. K., Mancebo, H., Lane, W. S., Flores, O., & Reinberg, D. (1999). A protein phosphatase functions to recycle RNA polymerase II. Genes and Development, 13(12), 1540-1552.

A protein phosphatase functions to recycle RNA polymerase II. / Cho, Helen; Kim, Tae Kyung; Mancebo, Helena; Lane, William S.; Flores, Osvaldo; Reinberg, Danny.

In: Genes and Development, Vol. 13, No. 12, 15.06.1999, p. 1540-1552.

Research output: Contribution to journalArticle

Cho, H, Kim, TK, Mancebo, H, Lane, WS, Flores, O & Reinberg, D 1999, 'A protein phosphatase functions to recycle RNA polymerase II', Genes and Development, vol. 13, no. 12, pp. 1540-1552.
Cho H, Kim TK, Mancebo H, Lane WS, Flores O, Reinberg D. A protein phosphatase functions to recycle RNA polymerase II. Genes and Development. 1999 Jun 15;13(12):1540-1552.
Cho, Helen ; Kim, Tae Kyung ; Mancebo, Helena ; Lane, William S. ; Flores, Osvaldo ; Reinberg, Danny. / A protein phosphatase functions to recycle RNA polymerase II. In: Genes and Development. 1999 ; Vol. 13, No. 12. pp. 1540-1552.
@article{49fc9a0dff2b422c96c873f12da7df2d,
title = "A protein phosphatase functions to recycle RNA polymerase II",
abstract = "Transcription is regulated by the state of phosphorylation of a heptapeptide repeat known as the carboxy-terminal domain (CTD) present in the largest subunit of RNA polymerase II (RNAPII). RNAPII that associates with transcription initiation complexes contains an unphosphorylated CTD, whereas the elongating polymerase has a phosphorylated CTD. Transcription factor IIH has a kinase activity specific for the CTD that is stimulated by the formation of a transcription initiation complex. Here, we report the isolation of a cDNA clone encoding a 150-kD polypeptide, which, together with RNAPII, reconstitutes a highly specific CTD phosphatase activity. Functional analysis demonstrates that the CTD phosphatase allows recycling of RNAPII. The phosphatase dephosphorylates the CTD allowing efficient incorporation of RNAPII into transcription initiation complexes, which results in increased transcription. The CTD phosphatase was found to be active in ternary elongation complexes. Moreover, the phosphatase stimulates elongation by RNAPII; however, this function is independent of its catalytic activity.",
keywords = "CTD phosphatase, Phosphorylation, RNA polymerase II, Transcription",
author = "Helen Cho and Kim, {Tae Kyung} and Helena Mancebo and Lane, {William S.} and Osvaldo Flores and Danny Reinberg",
year = "1999",
month = "6",
day = "15",
language = "English (US)",
volume = "13",
pages = "1540--1552",
journal = "Genes and Development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "12",

}

TY - JOUR

T1 - A protein phosphatase functions to recycle RNA polymerase II

AU - Cho, Helen

AU - Kim, Tae Kyung

AU - Mancebo, Helena

AU - Lane, William S.

AU - Flores, Osvaldo

AU - Reinberg, Danny

PY - 1999/6/15

Y1 - 1999/6/15

N2 - Transcription is regulated by the state of phosphorylation of a heptapeptide repeat known as the carboxy-terminal domain (CTD) present in the largest subunit of RNA polymerase II (RNAPII). RNAPII that associates with transcription initiation complexes contains an unphosphorylated CTD, whereas the elongating polymerase has a phosphorylated CTD. Transcription factor IIH has a kinase activity specific for the CTD that is stimulated by the formation of a transcription initiation complex. Here, we report the isolation of a cDNA clone encoding a 150-kD polypeptide, which, together with RNAPII, reconstitutes a highly specific CTD phosphatase activity. Functional analysis demonstrates that the CTD phosphatase allows recycling of RNAPII. The phosphatase dephosphorylates the CTD allowing efficient incorporation of RNAPII into transcription initiation complexes, which results in increased transcription. The CTD phosphatase was found to be active in ternary elongation complexes. Moreover, the phosphatase stimulates elongation by RNAPII; however, this function is independent of its catalytic activity.

AB - Transcription is regulated by the state of phosphorylation of a heptapeptide repeat known as the carboxy-terminal domain (CTD) present in the largest subunit of RNA polymerase II (RNAPII). RNAPII that associates with transcription initiation complexes contains an unphosphorylated CTD, whereas the elongating polymerase has a phosphorylated CTD. Transcription factor IIH has a kinase activity specific for the CTD that is stimulated by the formation of a transcription initiation complex. Here, we report the isolation of a cDNA clone encoding a 150-kD polypeptide, which, together with RNAPII, reconstitutes a highly specific CTD phosphatase activity. Functional analysis demonstrates that the CTD phosphatase allows recycling of RNAPII. The phosphatase dephosphorylates the CTD allowing efficient incorporation of RNAPII into transcription initiation complexes, which results in increased transcription. The CTD phosphatase was found to be active in ternary elongation complexes. Moreover, the phosphatase stimulates elongation by RNAPII; however, this function is independent of its catalytic activity.

KW - CTD phosphatase

KW - Phosphorylation

KW - RNA polymerase II

KW - Transcription

UR - http://www.scopus.com/inward/record.url?scp=0033564705&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033564705&partnerID=8YFLogxK

M3 - Article

VL - 13

SP - 1540

EP - 1552

JO - Genes and Development

JF - Genes and Development

SN - 0890-9369

IS - 12

ER -