Title |
Structural and Functional Analysis of Essential pre-mRNA Splicing Factor Prp19p
|
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Published in |
Molecular & Cellular Biology, March 2023
|
DOI | 10.1128/mcb.25.1.451-460.2005 |
Pubmed ID | |
Authors |
Melanie D. Ohi, Craig W. Vander Kooi, Joshua A. Rosenberg, Liping Ren, Justin P. Hirsch, Walter J. Chazin, Thomas Walz, Kathleen L. Gould |
Abstract |
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. |
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