Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 25, Issue 1, Pages 451-460Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.25.1.451-460.2005
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Funding
- NATIONAL CANCER INSTITUTE [T32CA009385] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM008320, P01GM062580, R01GM062112] Funding Source: NIH RePORTER
- NCI NIH HHS [T32 CA 09385, T32 CA009385] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008320, P01 GM062580, R01 GM 62112, T32 GM 08320, R01 GM062112] Funding Source: Medline
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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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