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| | ==Second zinc-binding domain from yeast Pcf11== | | ==Second zinc-binding domain from yeast Pcf11== |
| - | <StructureSection load='5m9z' size='340' side='right'caption='[[5m9z]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='5m9z' size='340' side='right'caption='[[5m9z]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m9z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M9Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m9z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M9Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCF11, YDR228C, YD9934.13C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9z OCA], [http://pdbe.org/5m9z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m9z RCSB], [http://www.ebi.ac.uk/pdbsum/5m9z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9z ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9z OCA], [https://pdbe.org/5m9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m9z RCSB], [https://www.ebi.ac.uk/pdbsum/5m9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PCF11_YEAST PCF11_YEAST]] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.<ref>PMID:11344258</ref> <ref>PMID:15998810</ref> | + | [https://www.uniprot.org/uniprot/PCF11_YEAST PCF11_YEAST] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.<ref>PMID:11344258</ref> <ref>PMID:15998810</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mackereth, C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mrna]] | + | [[Category: Mackereth C]] |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rna processing]]
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| - | [[Category: Zinc-binding]]
| + | |
| Structural highlights
Function
PCF11_YEAST Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.[1] [2]
Publication Abstract from PubMed
New transcripts generated by RNA polymerase II (RNAPII) are generally processed in order to form mature mRNAs. Two key processing steps include a precise cleavage within the 3' end of the pre-mRNA, and the subsequent polymerization of adenosines to produce the poly(A) tail. In yeast, these two functions are performed by a large multi-subunit complex that includes the Cleavage Factor IA (CF IA). The four proteins Pcf11, Clp1, Rna14 and Rna15 constitute the yeast CF IA, and of these, Pcf11 is structurally the least characterized. Here, we provide evidence for the binding of two Zn2+ atoms to Pcf11, bound to separate zinc-binding domains located on each side of the Clp1 recognition region. Additional structural characterization of the second zinc-binding domain shows that it forms an unusual zinc finger fold. We further demonstrate that the two domains are not mandatory for CF IA assembly nor RNA polymerase II transcription termination, but are rather involved to different extents in the pre-mRNA 3'-end processing mechanism. Our data thus contribute to a more complete understanding of the architecture and function of Pcf11 and its role within the yeast CF IA complex.
Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.,Guegueniat J, Dupin AF, Stojko J, Beaurepaire L, Cianferani S, Mackereth CD, Minvielle-Sebastia L, Fribourg S Nucleic Acids Res. 2017 Sep 29;45(17):10115-10131. doi: 10.1093/nar/gkx674. PMID:28973460[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gross S, Moore C. Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6080-5. Epub 2001 May 8. PMID:11344258 doi:http://dx.doi.org/10.1073/pnas.101046598
- ↑ Zhang Z, Fu J, Gilmour DS. CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 3'-end processing factor, Pcf11. Genes Dev. 2005 Jul 1;19(13):1572-80. PMID:15998810 doi:http://dx.doi.org/19/13/1572
- ↑ Guegueniat J, Dupin AF, Stojko J, Beaurepaire L, Cianferani S, Mackereth CD, Minvielle-Sebastia L, Fribourg S. Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing. Nucleic Acids Res. 2017 Sep 29;45(17):10115-10131. doi: 10.1093/nar/gkx674. PMID:28973460 doi:http://dx.doi.org/10.1093/nar/gkx674
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