Crystal structure of the human symplekin–Ssu72–CTD phosphopeptide complex

Kehui Xiang, Takashi Nagaike, Song Xiang, Turgay Kilic, Maia M. Beh, James L. Manley and Liang Tong ()
Additional contact information
Kehui Xiang: Columbia University
Takashi Nagaike: Columbia University
Song Xiang: Columbia University
Turgay Kilic: Columbia University
Maia M. Beh: Columbia University
James L. Manley: Columbia University
Liang Tong: Columbia University

Nature, 2010, vol. 467, issue 7316, 729-733

Abstract: Human symplekin structure The scaffolding protein symplekin (known as Pta1 in yeast) interacts with RNA polymerase II (RNA Pol II) and affects the initiation and termination of transcription. It is also involved in cleavage and polyadenylation at the 3′ end of mRNA precursors. Liang Tong and colleagues have now solved the structure of a ternary complex consisting of human symplekin, a short peptide (CTD-pSer5) mimicking the phosphorylated C-terminal tail of RNA Pol II, and Ssu72, which dephosphorylates this residue. The structure suggests a mechanism by which symplekin stimulates Ssu72's phosphatase activity, and reveals an unexpected cis configuration of the pSer5–Pro6 bond. The structure also explains how Ssu72 binding can facilitate polyadenylation activity when 3′ end processing is coupled to transcription.

Date: 2010
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DOI: 10.1038/nature09391

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