CTD Tyrosine Phosphorylation Impairs Termination Factor Recruitment to RNA Polymerase II

In different phases of the transcription cycle, RNA polymerase (Pol) II recruits various factors via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the sequence Tyr¹-Ser²-Pro³-Thr⁴ -Ser⁵ -Pro⁶ -Ser⁷. We show that the CTD of transcribing yeast Pol II is phosphoryla...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2012-06, Vol.336 (6089), p.1723-1725
Main Authors: Mayer, Andreas, Heidemann, Martin, Lidschreiber, Michael, Schreieck, Amelie, Sun, Mai, Hintermair, Corinna, Kremmer, Elisabeth, Eick, Dirk, Cramer, Patrick
Format: Article
Language:English
Subjects:
Amino acids
Antibodies
Biochemistry
Biological and medical sciences
Catalytic Domain
Charge transfer devices
Chromatin Immunoprecipitation
Elongation
Enzymes
Fluorescence
Fundamental and applied biological sciences. Psychology
Genes
HeLa Cells
Humans
Messenger RNA
Molecular and cellular biology
Molecular genetics
Open reading frames
Peptide elongation factors
Peptide Termination Factors - metabolism
Phosphorylation
Polymerase
Protein Kinases - metabolism
Recruitment
Residues
Ribonucleic acids
RNA
RNA polymerase
RNA Polymerase II - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - metabolism
Transcription. Transcription factor. Splicing. Rna processing
Transcriptional Elongation Factors - metabolism
Tyrosine
Tyrosine - metabolism
Yeasts
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In different phases of the transcription cycle, RNA polymerase (Pol) II recruits various factors via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the sequence Tyr¹-Ser²-Pro³-Thr⁴ -Ser⁵ -Pro⁶ -Ser⁷. We show that the CTD of transcribing yeast Pol II is phosphorylated at Tyr¹, in addition to Ser², Thr⁴, Ser⁵, and Ser⁷. Tyr¹ phosphorylation stimulates binding of elongation factor Spt6 and impairs recruitment of termination factors Nrd1, Pcf11, and Rtt103. Tyr¹ phosphorylation levels rise downstream of the transcription start site and decrease before the polyadenylation site, largely excluding termination factors from gene bodies. These results show that CTD modifications trigger and block factor recruitment and lead to an extended CTD code that explains transcription cycle coordination on the basis of differential phosphorylation of Tyr¹, Ser², and Ser⁵.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1219651