Structural insights into mechanisms of the small RNA methyltransferase HEN1

Ying Huang, Lijuan Ji, Qichen Huang, Dmitry G. Vassylyev, Xuemei Chen and Jin-Biao Ma ()
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Ying Huang: Schools of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA
Lijuan Ji: Institute of Integrative Genome Biology, University of California, Riverside, California 92521, USA
Qichen Huang: Schools of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA
Dmitry G. Vassylyev: Schools of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA
Xuemei Chen: Institute of Integrative Genome Biology, University of California, Riverside, California 92521, USA
Jin-Biao Ma: Schools of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA

Nature, 2009, vol. 461, issue 7265, 823-827

Abstract: Small RNAs are HEN-picked Some of the small RNAs involved in RNA silencing require addition on their 3′ terminal nucleotide of a 2′-O-methyl group in order for the precursor RNA to be processed correctly. This modification is performed by the HEN1 RNA methyltransferase, using AdoMet as a methyl donor. In this study, Ma and colleagues have solved the structure of a plant HEN1 in complex with an RNA duplex and the cofactor product, AdoHcy. The structure reveals how the enzyme recognizes the correct substrate and suggests a new mechanism for methylation.

Date: 2009
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DOI: 10.1038/nature08433

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