Solution structures of the double-stranded RNA-binding domains from RNA helicase A.

Takashi Nagata, Kengo Tsuda, Naohiro Kobayashi, Mikako Shirouzu, Takanori Kigawa, Peter Güntert, Shigeyuki Yokoyama, Yutaka Muto

Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.

Proteins 2012 Jun

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RNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex. We present the first solution structures of the double-stranded RNA-binding domains (dsRBDs), dsRBD1 and dsRBD2, from mouse RHA. We discuss the binding mode of the dsRBDs of RHA, in comparison with the known dsRBD structures in their complexes. Our structural data provide important information for the elucidation of the molecular reassembly mediated by RHA. Copyright © 2012 Wiley Periodicals, Inc.

Citation

Takashi Nagata, Kengo Tsuda, Naohiro Kobayashi, Mikako Shirouzu, Takanori Kigawa, Peter Güntert, Shigeyuki Yokoyama, Yutaka Muto. Solution structures of the double-stranded RNA-binding domains from RNA helicase A. Proteins. 2012 Jun;80(6):1699-706