She2p is a novel RNA binding protein with a basic helical hairpin motif

Dierk Niessing, Stefan Hüttelmaier, Daniel Zenklusen, Robert H. Singer, Stephen K. Burley

Research output: Contribution to journalArticle

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Abstract

Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures asymmetric distribution of information within and among eukaryotic cells. Actin-dependent transport of ASH1 mRNA in yeast represents one of the best-characterized examples of mRNP translocation. Formation of the ASH1 mRNP requires recognition of zip code elements by the RNA binding protein She2p. We determined the X-ray structure of She2p at 1.95 Å resolution. She2p is a member of a previously unknown class of nucleic acid binding proteins, composed of a single globular domain with a five α helix bundle that forms a symmetric homodimer. After demonstrating potent, dimer-dependent RNA binding in vitro, we mapped the RNA binding surface of She2p to a basic helical hairpin in vitro and in vivo and present a mechanism for mRNA-dependent initiation of ASH1 mRNP complex assembly.

Original languageEnglish (US)
Pages (from-to)491-502
Number of pages12
JournalCell
Volume119
Issue number4
DOIs
StatePublished - Nov 12 2004

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Niessing, D., Hüttelmaier, S., Zenklusen, D., Singer, R. H., & Burley, S. K. (2004). She2p is a novel RNA binding protein with a basic helical hairpin motif. Cell, 119(4), 491-502. https://doi.org/10.1016/j.cell.2004.10.018