한빛사논문
- 조회3,474
Abstract
Jeong Ho Chang1,3, Song Xiang1-3, Kehui Xiang1, James L Manley1 & Liang Tong1
1Department of Biological Sciences, Columbia University, New York, New York, USA. 2Present address: Key Laboratory of Nutrition and Metabolism, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, P.R. China. 3These authors contributed equally to this work.
Correspondence should be addressed to L.T.
The 5′→3′ exoribonucleases (XRNs) have important functions in transcription, RNA metabolism and RNA interference. The structure of Rat1 (also known as Xrn2) showed that the two highly conserved regions of XRNs form a single, large domain that defines the active site of the enzyme. Xrn1 has a 510-residue segment after the conserved regions that is required for activity but is absent from Rat1/Xrn2. Here we report the crystal structures of Kluyveromyces lactis Xrn1 (residues 1.1,245, E178Q mutant), alone and in complex with a Mn2+ ion in the active site. The 510-residue segment contains four domains (D1.D4), located far from the active site. Our mutagenesis and biochemical studies show that their functional importance results from their ability to stabilize the conformation of the N-terminal segment of Xrn1. These domains might also constitute a platform that interacts with protein partners of Xrn1.
논문정보
- Research article
- 2011년 02월 (BRIC 등록일 )
- 국외 연구진
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