Abstract
RNA helicase A (RHA) is a multifunctional protein that regulates gene expression. RHA has two double-stranded RNA-binding domains (dsRBDs) that serve as modules for highly structured RNA binding and protein–protein interactions. Using the dsRBDs, RHA binds to cellular and viral mRNAs, exports them from the nucleus, and regulates splicing as well as translational initiation. The RHA dsRBDs also reportedly mediate interactions with small RNAs and other dsRBD-containing proteins, and altogether form a processing complex involved in RNA silencing pathways. In addition, the RHA dsRBDs bridge RNA polymerase II with several transcription factors. Here we report the 1H, 13C, and 15N chemical shift assignments of the dsRBDs of RHA. The resonance assignments obtained in this work will contribute to the elucidation of the interactions between RHA and transcriptional or post-transcriptional gene regulators.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD (1998) BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nat Genet 19:254–256
Bolinger C, Sharma A, Singh D, Yu L, Boris-Lawrie K (2010) RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions. Nucleic Acids Res 38:1686–1696
Chendrimada TP, Gregory RI, Kumaraswamy E, Norman J, Cooch N, Nishikura K, Shiekhattar R (2005) TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing. Nature 436:740–744
Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Gruter P, Tabernero C, von Kobbe C, Schmitt C, Saavedra C, Bachi A, Wilm M, Felber BK, Izaurralde E (1998) TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol Cell 1:649–659
Haase AD, Jaskiewicz L, Zhang H, Laine S, Sack R, Gatignol A, Filipowicz W (2005) TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing. EMBO Rep 6:961–967
Hammond SM, Boettcher S, Caudy AA, Kobayashi R, Hannon GJ (2001) Argonaute2, a link between genetic and biochemical analyses of RNAi. Science 293:1146–1150
Hartman TR, Qian S, Bolinger C, Fernandez S, Schoenberg DR, Boris-Lawrie K (2006) RNA helicase A is necessary for translation of selected messenger RNAs. Nat Struct Mol Biol 13:509–516
Hull S, Boris-Lawrie K (2003) Analysis of synergy between divergent simple retrovirus posttranscriptional control elements. Virology 317:146–154
Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352
Kigawa T, Yabuki T, Matsuda N, Matsuda T, Nakajima R, Tanaka A, Yokoyama S (2004) Preparation of Escherichia coli cell extract for highly productive cell-free protein expression. J Struct Funct Genomics 5:63–68
Kobayashi N, Iwahara J, Koshiba S, Tomizawa T, Tochio N, Güntert P, Kigawa T, Yokoyama S (2007) KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. J Biomol NMR 39:31–52
Lee CG, Hurwitz J (1992) A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3′ to 5′ direction. J Biol Chem 267:4398–4407
Nagata T, Suzuki S, Endo R, Shirouzu M, Terada T, Inoue M, Kigawa T, Kobayashi N, Güntert P, Tanaka A, Hayashizaki Y, Muto Y, Yokoyama S (2008) The RRM domain of poly(A)-specific ribonuclease has a noncanonical binding site for mRNA cap analog recognition. Nucleic Acids Res 36:4754–4767
Nakajima T, Uchida C, Anderson SF, Lee CG, Hurwitz J, Parvin JD, Montminy M (1997) RNA helicase A mediates association of CBP with RNA polymerase II. Cell 90:1107–1112
Sadler AJ, Latchoumanin O, Hawkes D, Mak J, Williams BR (2009) An antiviral response directed by PKR phosphorylation of the RNA helicase A. PLoS Pathog 5:e1000311
Siomi H, Siomi MC (2009) On the road to reading the RNA-interference code. Nature 457:396–404
Tang H, Wong-Staal F (2000) Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus. J Biol Chem 275:32694–32700
Tang H, Gaietta GM, Fischer WH, Ellisman MH, Wong-Staal F (1997) A cellular cofactor for the constitutive transport element of type D retrovirus. Science 276:1412–1415
Tettweiler G, Lasko P (2006) A new model for translational regulation of specific mRNAs. Trends Biochem Sci 31:607–610
Acknowledgments
We are grateful to Natsuko Matsuda, Yoko Motoda, Atsuo Kobayashi, Masaru Hanada, Masaomi Ikari, Fumiko Hiroyasu, Miyuki Sato, Satoko Yasuda, Yuri Tsuboi, Yasuko Tomo, Yukiko Fujikura, Takeshi Nagira, Hiroko Uda-Tochio, and Yukiko Kinoshita-Sakaguchi for sample preparation. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI), the National Project on Protein Structural and Functional Analyses of the Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT). T.N. acknowledges financial support by the Ministry of Education, Culture, Sports, Science and Technology of Japan (Grants-in-Aid for Scientific Research: 23570146 and 21370047) and Advanced Medical Research Center of Yokohama City University. P.G. acknowledges financial support by the Lichtenberg program of the Volkswagen Foundation and by the Japan Society for the Promotion of Science (JSPS).
Author information
Authors and Affiliations
Corresponding authors
Rights and permissions
About this article
Cite this article
Nagata, T., Tsuda, K., Kobayashi, N. et al. 1H, 13C, and 15N resonance assignments of the dsRBDs of mouse RNA helicase A. Biomol NMR Assign 7, 69–72 (2013). https://doi.org/10.1007/s12104-012-9380-3
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12104-012-9380-3