Prp40: Difference between revisions
New page: == Structure of Prp40 == by Kelly Hrywkiw {{STRUCTURE_1o6w | PDB=1o6w | SCENE= scene name='Sandbox_504/Start_scene/1'}} __TOC__ =Introduction= Prp40 has been implicated in early... |
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=Introduction= | =Introduction= | ||
Prp40 has been implicated in early steps of [http://en.wikipedia.org/wiki/Spliceosome spliceosomal] assembly, and binding to the phosphorylated C-terminal domain (phospho-CTD) of [http://en.wikipedia.org/wiki/RNA_polymerase_II RNA polymerase II] (RNAPII)<ref name ="bonet">PMID:19722265</ref>. Two types of domains are found in Prp40, two [http://en.wikipedia.org/wiki/WW_domain WW] and six consecutive FF domains<ref name ="wiesner">PMID:12460579</ref>. WW domains contain two highly conserved tyrosine residues that bind to proline rich sequences, thereby mediating protein-protein interactions<ref name ="wiesner"/>. Both WW domains of Prp40 can interact with PPxY motifs (x is any residue) and PPѰѰP motifs (Ѱ is an aliphatic residue)<ref name ="wiesner"/>. FF domains contain two highly conserved proline residues and can be found in arrays up to six domains<ref name ="gasch">PMID:16253993</ref>. Interestingly, these tandem domains appear not to function in co-operative binding, rather they may provide multiple independent binding sites<ref name ="gasch"/>. With regards to interactions between the different domains, the WW domains bind to the splicing protein: branch point-binding protein (BBP, also known as Ms15 and ySF1) and Prp8; the FF domains interact with the splicing factor Clf1 (Syf3p in yeast), and the phospho-CTD of RNAPII<ref name ="gasch"/><ref name ="wiesner"/>. | '''Prp40''' has been implicated in early steps of [http://en.wikipedia.org/wiki/Spliceosome spliceosomal] assembly, and binding to the phosphorylated C-terminal domain (phospho-CTD) of [http://en.wikipedia.org/wiki/RNA_polymerase_II RNA polymerase II] (RNAPII)<ref name ="bonet">PMID:19722265</ref>. Two types of domains are found in Prp40, two [http://en.wikipedia.org/wiki/WW_domain WW] and six consecutive FF domains<ref name ="wiesner">PMID:12460579</ref>. WW domains contain two highly conserved tyrosine residues that bind to proline rich sequences, thereby mediating protein-protein interactions<ref name ="wiesner"/>. Both WW domains of Prp40 can interact with PPxY motifs (x is any residue) and PPѰѰP motifs (Ѱ is an aliphatic residue)<ref name ="wiesner"/>. FF domains contain two highly conserved proline residues and can be found in arrays up to six domains<ref name ="gasch">PMID:16253993</ref>. Interestingly, these tandem domains appear not to function in co-operative binding, rather they may provide multiple independent binding sites<ref name ="gasch"/>. With regards to interactions between the different domains, the WW domains bind to the splicing protein: branch point-binding protein (BBP, also known as Ms15 and ySF1) and Prp8; the FF domains interact with the splicing factor Clf1 (Syf3p in yeast), and the phospho-CTD of RNAPII<ref name ="gasch"/><ref name ="wiesner"/>. | ||
=Role in spliceosomal assembly= | =Role in spliceosomal assembly= | ||