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

Jing-Ping Hsin, Amit Sheth, James L Manley

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

Science (New York, N.Y.) 2011 Nov 4

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The RNA polymerase II (RNAP II) largest subunit contains a C-terminal domain (CTD) with up to 52 Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7) consensus repeats. Serines 2, 5, and 7 are known to be phosphorylated, and these modifications help to orchestrate the interplay between transcription and processing of messenger RNA (mRNA) precursors. Here, we provide evidence that phosphorylation of CTD Thr(4) residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes. Like Ser(2), Thr(4) phosphorylation requires the CTD kinase CDK9 and is evolutionarily conserved from yeast to human. Our data thus illustrate how a CTD modification can play a highly specific role in facilitating efficient gene expression.

Citation

Jing-Ping Hsin, Amit Sheth, James L Manley. RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3' end processing. Science (New York, N.Y.). 2011 Nov 4;334(6056):683-6