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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

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

Substances

  • ASH1 protein, S cerevisiae
  • DNA-Binding Proteins
  • RNA, Fungal
  • RNA, Messenger
  • RNA-Binding Proteins
  • Repressor Proteins
  • SHE2 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins

Associated data

  • PDB/1XLY