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

Author

Listed:
  • Kehui Xiang

    (Columbia University)

  • Takashi Nagaike

    (Columbia University)

  • Song Xiang

    (Columbia University
    Present address: Key Laboratory of Nutrition and Metabolism, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.)

  • Turgay Kilic

    (Columbia University)

  • Maia M. Beh

    (Columbia University)

  • James L. Manley

    (Columbia University)

  • Liang Tong

    (Columbia University)

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.

Suggested Citation

  • Kehui Xiang & Takashi Nagaike & Song Xiang & Turgay Kilic & Maia M. Beh & James L. Manley & Liang Tong, 2010. "Crystal structure of the human symplekin–Ssu72–CTD phosphopeptide complex," Nature, Nature, vol. 467(7316), pages 729-733, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7316:d:10.1038_nature09391
    DOI: 10.1038/nature09391
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    Cited by:

    1. David Flores-Solis & Irina P. Lushpinskaia & Anton A. Polyansky & Arya Changiarath & Marc Boehning & Milana Mirkovic & James Walshe & Lisa M. Pietrek & Patrick Cramer & Lukas S. Stelzl & Bojan Zagrovi, 2023. "Driving forces behind phase separation of the carboxy-terminal domain of RNA polymerase II," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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