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RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3' end processing

Jing-Ping Hsin1, Amit Sheth, James L Manley

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

Science (New York, N.Y.)
|November 5, 2011
PubMed

Insights

Phosphorylation of RNA polymerase II C-terminal domain (CTD) Thr(4) is crucial for histone mRNA processing. This modification, requiring CDK9, helps recruit processing factors to histone genes for efficient gene expression.

Area of Science:

  • Molecular Biology
  • Gene Expression Regulation

Background:

  • The RNA polymerase II C-terminal domain (CTD) features repeats with key phosphorylation sites.
  • Serine 2, 5, and 7 phosphorylations regulate transcription and mRNA precursor processing.

Purpose of the Study:

  • To investigate the role of CTD Thr(4) phosphorylation in gene expression.
  • To determine if Thr(4) phosphorylation is involved in specific mRNA processing events.

Main Methods:

  • Investigated CTD phosphorylation patterns in relation to mRNA processing.
  • Utilized genetic and biochemical approaches to study the function of CTD Thr(4) phosphorylation.
  • Examined the evolutionary conservation of Thr(4) phosphorylation.

Main Results:

  • CTD Thr(4) phosphorylation is specifically required for histone mRNA 3' end processing.
  • Thr(4) phosphorylation facilitates the recruitment of 3' processing factors to histone genes.
  • This modification requires the CTD kinase CDK9 and is conserved across species.

Conclusions:

  • CTD Thr(4) phosphorylation plays a specific role in histone gene expression.
  • This modification is essential for efficient histone mRNA processing and factor recruitment.
  • CTD modifications offer a mechanism for fine-tuning gene expression.

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