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Article
Nature Structural & Molecular Biology 13, 509 - 516 (2006)
Published online: 7 May 2006; Corrected online: 14 May 2006 | doi:10.1038/nsmb1092

RNA helicase A is necessary for translation of selected messenger RNAs

Tiffiney Roberts Hartman1, 6, 7, Shuiming Qian1, 2, 7, Cheryl Bolinger1, 2, Soledad Fernandez3, 4, Daniel R Schoenberg2, 4, 5 & Kathleen Boris-Lawrie1, 2, 4

1  Center for Retrovirus Research and Department of Veterinary Biosciences, The Ohio State University, Columbus, Ohio 43210 USA.

2  Molecular, Cellular & Developmental Biology Graduate Program, The Ohio State University, Columbus, Ohio 43210 USA.

3  Center for Biostatistics, The Ohio State University, Columbus, Ohio 43210 USA.

4  Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43210 USA.

5  Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210 USA.

6  Present address: Fox Chase Cancer Center, 333 Cottman Ave., Philadelphia, Pennsylvania 19111, USA.

7  These authors contributed equally to this work.

Correspondence should be addressed to Kathleen Boris-Lawrie boris-lawrie.1@osu.edu

RNA helicase A (RHA) is a highly conserved DEAD-box protein that activates transcription, modulates RNA splicing and binds the nuclear pore complex. The life cycle of typical mRNA involves RNA processing and translation after ribosome scanning of a relatively unstructured 5' untranslated region (UTR). The precursor RNAs of retroviruses and selected cellular genes harbor a complex 5' UTR and use a yet-to-be-identified host post-transcriptional effector to stimulate efficient translation. Here we show that RHA recognizes a structured 5'-terminal post-transcriptional control element (PCE) of a retrovirus and the JUND growth-control gene. RHA interacts with PCE RNA in the nucleus and cytoplasm, facilitates polyribosome association and is necessary for its efficient translation. Our results reveal a previously unidentified role for RHA in translation and implicate RHA as an integrative effector in the continuum of gene expression from transcription to translation.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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