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

Melanie D. Ohi, Craig W. Vander Kooi, Joshua A. Rosenberg, Liping Ren, Justin P. Hirsch, Walter J. Chazin, Thomas Walz, Kathleen L. Gould

Research output: Contribution to journalArticlepeer-review

75 Scopus citations


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.

Original languageEnglish
Pages (from-to)451-460
Number of pages10
JournalMolecular and Cellular Biology
Issue number1
StatePublished - Jan 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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