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Structure and function of the 5′→3′ exoribonuclease Rat1 and its activating partner Rai1

Author

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  • Song Xiang

    (Columbia University, New York, New York 10027, USA)

  • Amalene Cooper-Morgan

    (Columbia University, New York, New York 10027, USA)

  • Xinfu Jiao

    (Rutgers University, Piscataway, New Jersey 08854, USA)

  • Megerditch Kiledjian

    (Rutgers University, Piscataway, New Jersey 08854, USA)

  • James L. Manley

    (Columbia University, New York, New York 10027, USA)

  • Liang Tong

    (Columbia University, New York, New York 10027, USA)

Abstract

Exoribonucleases in yeast Exoribonucleases are important processing enzymes in many aspects of RNA metabolism. The activity of yeast Rat1, a 5′–3′ exonuclease, is stimulated by Rai1. In this work, Liang Tong and colleagues report the structures of two complexes: Rat1–Rai1 and DOM3Z (the mouse Rat1 homologue)–Rai1. These structures reveal the mechanism of exonuclease activity and define the catalytic differences with another class of nucleases containing a PIN domain. In addition, the work reveals that Rai1 has pyrophosphohydrolase activity, the first such activity found in eukaryotes.

Suggested Citation

  • Song Xiang & Amalene Cooper-Morgan & Xinfu Jiao & Megerditch Kiledjian & James L. Manley & Liang Tong, 2009. "Structure and function of the 5′→3′ exoribonuclease Rat1 and its activating partner Rai1," Nature, Nature, vol. 458(7239), pages 784-788, April.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7239:d:10.1038_nature07731
    DOI: 10.1038/nature07731
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    Cited by:

    1. Konstantin Axt & Sarah L French & Ann L Beyer & David Tollervey, 2014. "Kinetic Analysis Demonstrates a Requirement for the Rat1 Exonuclease in Cotranscriptional Pre-rRNA Cleavage," PLOS ONE, Public Library of Science, vol. 9(2), pages 1-11, February.
    2. Tatsuo Yanagisawa & Yuko Murayama & Haruhiko Ehara & Mie Goto & Mari Aoki & Shun-ichi Sekine, 2024. "Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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