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Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy.

The U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP) is a major, evolutionarily highly conserved spliceosome subunit. Unwinding of its U4/U6 snRNA duplex is a central event of spliceosome activation that requires several components of the U5 portion of the tri-snRNP, including the RNA helicase Brr2, Prp8 and the GTPase Snu114. Here we report the EM projection structure of the Saccharomyces cerevisiae tri-snRNP. It shows a modular organization comprising three extruding domains that contact one another in its central portion. We have visualized genetically tagged tri-snRNP proteins by EM and show here that U4/U6 snRNP forms a domain termed the arm. Conversely, a separate head domain adjacent to the arm harbors Brr2, whereas Prp8 and the GTPase Snu114 are located centrally. The head and arm adopt variable relative positions. This molecular organization and dynamics suggest possible scenarios for structural events during catalytic activation.

Pubmed ID: 18953335

Authors

  • Häcker I
  • Sander B
  • Golas MM
  • Wolf E
  • Karagöz E
  • Kastner B
  • Stark H
  • Fabrizio P
  • Lührmann R

Journal

Nature structural & molecular biology

Publication Data

November 5, 2008

Associated Grants

None

Mesh Terms

  • Enzyme Activation
  • Macromolecular Substances
  • Microscopy, Electron
  • Nucleic Acid Conformation
  • Protein Conformation
  • RNA Helicases
  • Ribonucleoprotein, U4-U6 Small Nuclear
  • Ribonucleoprotein, U5 Small Nuclear
  • Ribonucleoproteins, Small Nuclear
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Spliceosomes