Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination

David W. Zhang, Amber Mosley, Sreenivasa R. Ramisetty, Juan B. Rodríguez-Molina, Michael P. Washburn, Aseem Z. Ansari

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks is well explored, genome-wide engagement of phosphatases that remove these CTD marks is poorly understood. In particular, identifying the enzyme that erases phospho- Ser7 (Ser7-P) marks is especially important, because we find that substituting this residue with a glutamate, a phosphomimic, is lethal. Our observations implicate Ssu72 as a Ser7-P phosphatase. We report that removal of all phospho-CTD marks during transcription termination is mechanistically coupled. An inability to remove these marks prevents Pol II from terminating efficiently and will likely impede subsequent assembly into the pre-initiation complex.

Original languageEnglish
Pages (from-to)8541-8551
Number of pages11
JournalJournal of Biological Chemistry
Volume287
Issue number11
DOIs
StatePublished - Mar 9 2012

Fingerprint

RNA Polymerase III
Phosphorylation
RNA Polymerase II
Transcription
Phosphoric Monoester Hydrolases
Machinery
Glutamic Acid
Genes
Genome
Enzymes
RNA polymerase II largest subunit

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination. / Zhang, David W.; Mosley, Amber; Ramisetty, Sreenivasa R.; Rodríguez-Molina, Juan B.; Washburn, Michael P.; Ansari, Aseem Z.

In: Journal of Biological Chemistry, Vol. 287, No. 11, 09.03.2012, p. 8541-8551.

Research output: Contribution to journalArticle

Zhang, David W. ; Mosley, Amber ; Ramisetty, Sreenivasa R. ; Rodríguez-Molina, Juan B. ; Washburn, Michael P. ; Ansari, Aseem Z. / Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 11. pp. 8541-8551.
@article{dc8bdec285434765bda04c6fa4dcabf0,
title = "Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination",
abstract = "The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks is well explored, genome-wide engagement of phosphatases that remove these CTD marks is poorly understood. In particular, identifying the enzyme that erases phospho- Ser7 (Ser7-P) marks is especially important, because we find that substituting this residue with a glutamate, a phosphomimic, is lethal. Our observations implicate Ssu72 as a Ser7-P phosphatase. We report that removal of all phospho-CTD marks during transcription termination is mechanistically coupled. An inability to remove these marks prevents Pol II from terminating efficiently and will likely impede subsequent assembly into the pre-initiation complex.",
author = "Zhang, {David W.} and Amber Mosley and Ramisetty, {Sreenivasa R.} and Rodr{\'i}guez-Molina, {Juan B.} and Washburn, {Michael P.} and Ansari, {Aseem Z.}",
year = "2012",
month = "3",
day = "9",
doi = "10.1074/jbc.M111.335687",
language = "English",
volume = "287",
pages = "8541--8551",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

TY - JOUR

T1 - Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination

AU - Zhang, David W.

AU - Mosley, Amber

AU - Ramisetty, Sreenivasa R.

AU - Rodríguez-Molina, Juan B.

AU - Washburn, Michael P.

AU - Ansari, Aseem Z.

PY - 2012/3/9

Y1 - 2012/3/9

N2 - The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks is well explored, genome-wide engagement of phosphatases that remove these CTD marks is poorly understood. In particular, identifying the enzyme that erases phospho- Ser7 (Ser7-P) marks is especially important, because we find that substituting this residue with a glutamate, a phosphomimic, is lethal. Our observations implicate Ssu72 as a Ser7-P phosphatase. We report that removal of all phospho-CTD marks during transcription termination is mechanistically coupled. An inability to remove these marks prevents Pol II from terminating efficiently and will likely impede subsequent assembly into the pre-initiation complex.

AB - The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an important role in coordinating stage-specific recruitment and release of cellular machines during transcription. Dynamic placement and removal of phosphorylation marks on different residues of a repeating heptapeptide (YSPTSPS) of the CTD underlies the engagement of relevant cellular machinery. Whereas sequential placement of phosphorylation marks is well explored, genome-wide engagement of phosphatases that remove these CTD marks is poorly understood. In particular, identifying the enzyme that erases phospho- Ser7 (Ser7-P) marks is especially important, because we find that substituting this residue with a glutamate, a phosphomimic, is lethal. Our observations implicate Ssu72 as a Ser7-P phosphatase. We report that removal of all phospho-CTD marks during transcription termination is mechanistically coupled. An inability to remove these marks prevents Pol II from terminating efficiently and will likely impede subsequent assembly into the pre-initiation complex.

UR - http://www.scopus.com/inward/record.url?scp=84863229897&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84863229897&partnerID=8YFLogxK

U2 - 10.1074/jbc.M111.335687

DO - 10.1074/jbc.M111.335687

M3 - Article

C2 - 22235117

AN - SCOPUS:84863229897

VL - 287

SP - 8541

EP - 8551

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 11

ER -