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. 2004 Nov 12;119(4):491-502.
doi: 10.1016/j.cell.2004.10.018.

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

Dierk Niessing  1 , Stefan Hüttelmaier, Daniel Zenklusen, Robert H Singer, Stephen K Burley
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Free article

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

Dierk Niessing et al. Cell. .
Free article

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 A resolution. She2p is a member of a previously unknown class of nucleic acid binding proteins, composed of a single globular domain with a five alpha 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.

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