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

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.

Pubmed ID: 15537539

Authors

  • Niessing D
  • Hüttelmaier S
  • Zenklusen D
  • Singer RH
  • Burley SK

Journal

Cell

Publication Data

November 12, 2004

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM57071
  • Agency: NIGMS NIH HHS, Id: GM61262

Mesh Terms

  • Amino Acid Sequence
  • Conserved Sequence
  • DNA-Binding Proteins
  • Dimerization
  • Models, Molecular
  • Molecular Sequence Data
  • RNA, Fungal
  • RNA, Messenger
  • RNA-Binding Proteins
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins