TY - JOUR
T1 - Structural and functional analysis of essential pre-mRNA splicing factor Prp19p
AU - Ohi, Melanie D.
AU - Vander Kooi, Craig W.
AU - Rosenberg, Joshua A.
AU - Ren, Liping
AU - Hirsch, Justin P.
AU - Chazin, Walter J.
AU - Walz, Thomas
AU - Gould, Kathleen L.
PY - 2005/1
Y1 - 2005/1
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/11144320747
UR - https://www.scopus.com/pages/publications/11144320747#tab=citedBy
U2 - 10.1128/MCB.25.1.451-460.2005
DO - 10.1128/MCB.25.1.451-460.2005
M3 - Article
C2 - 15601865
AN - SCOPUS:11144320747
SN - 0270-7306
VL - 25
SP - 451
EP - 460
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
IS - 1
ER -