Structural and Functional Analysis of Essential pre-mRNA Splicing Factor Prp19p
AUTOR(ES)
Ohi, Melanie D.
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=538785Documentos Relacionados
- Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing
- Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains.
- Fission yeast Prp4p kinase regulates pre-mRNA splicing by phosphorylating a non-SR-splicing factor
- Functional analysis of the polypyrimidine tract in pre-mRNA splicing.
- The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase.
