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Genes Dev. 2012 Oct 15;26(20):2265-70. doi: 10.1101/gad.198853.112.

An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72.

Author information

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

Abstract

Ssu72, an RNA polymerase II C-terminal domain (CTD) phospho-Ser5 (pSer5) phosphatase, was recently reported to have pSer7 phosphatase activity as well. We report here the crystal structure of a ternary complex of the N-terminal domain of human symplekin, human Ssu72, and a 10-mer pSer7 CTD peptide. Surprisingly, the peptide is bound in the Ssu72 active site with its backbone running in the opposite direction compared with a pSer5 peptide. The pSer7 phosphatase activity of Ssu72 is ∼4000-fold lower than its pSer5 phosphatase activity toward a peptide substrate, consistent with the structural observations.

PMID:
23070812
PMCID:
PMC3475799
DOI:
10.1101/gad.198853.112
[Indexed for MEDLINE]
Free PMC Article

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