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Structural and functional analysis of essential pre-mRNA splicing factor Prp19p.

U-box-containing Prp19p is an integral component of the Prp19p-associated complex (the nineteen complex, or NTC) that is essential for activation of the spliceosome. Prp19p makes numerous protein-protein contacts with other NTC components and is required for NTC stability. Here we show that Prp19p forms a tetramer in vitro and in vivo and we map the domain required for its oligomerization to a central tetrameric coiled-coil. Biochemical and in vivo analyses are consistent with Prp19p tetramerization providing an interaction surface for a single copy of its binding partner, Cef1p. Electron microscopy showed that the isolated Prp19p tetramer is an elongated particle consisting of four globular WD40 domains held together by a central stalk consisting of four N-terminal U-boxes and four coiled-coils. These structural and functional data provide a basis for understanding the role of Prp19p as a key architectural component of the NTC.

Pubmed ID: 15601865


  • Ohi MD
  • Vander Kooi CW
  • Rosenberg JA
  • Ren L
  • Hirsch JP
  • Chazin WJ
  • Walz T
  • Gould KL


Molecular and cellular biology

Publication Data

January 16, 2005

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM 62112
  • Agency: NCI NIH HHS, Id: T32 CA 09385
  • Agency: NIGMS NIH HHS, Id: T32 GM 08320
  • Agency: NIGMS NIH HHS, Id: T32 GM008320

Mesh Terms

  • Cell Cycle Proteins
  • Chromatography, Gel
  • Circular Dichroism
  • DNA Mutational Analysis
  • Dimerization
  • Genotype
  • Image Processing, Computer-Assisted
  • Immunoblotting
  • Immunoprecipitation
  • Microscopy, Electron
  • Models, Biological
  • Polymerase Chain Reaction
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA Splicing
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Spliceosomes
  • Structure-Activity Relationship
  • Temperature
  • Two-Hybrid System Techniques
  • Ultracentrifugation