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

Song Xiang, Amalene Cooper-Morgan, Xinfu Jiao, Megerditch Kiledjian, James L. Manley and Liang Tong ()
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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

Nature, 2009, vol. 458, issue 7239, 784-788

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.

Date: 2009
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DOI: 10.1038/nature07731

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