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| | ==The conserved domain of yeast Cdc73== | | ==The conserved domain of yeast Cdc73== |
| - | <StructureSection load='4dm4' size='340' side='right' caption='[[4dm4]], [[Resolution|resolution]] 2.19Å' scene=''> | + | <StructureSection load='4dm4' size='340' side='right'caption='[[4dm4]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dm4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DM4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dm4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC73, YLR418C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | </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=4dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm4 OCA], [https://pdbe.org/4dm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm4 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm4 ProSAT]</span></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=4dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm4 OCA], [http://pdbe.org/4dm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dm4 RCSB], [http://www.ebi.ac.uk/pdbsum/4dm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CDC73_YEAST CDC73_YEAST]] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.<ref>PMID:9032243</ref> <ref>PMID:15643076</ref> <ref>PMID:16246725</ref> | + | [[https://www.uniprot.org/uniprot/CDC73_YEAST CDC73_YEAST]] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.<ref>PMID:9032243</ref> <ref>PMID:15643076</ref> <ref>PMID:16246725</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: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, H]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gao, Y]] | + | [[Category: Chen H]] |
| - | [[Category: Li, X]] | + | [[Category: Gao Y]] |
| - | [[Category: Niu, L]] | + | [[Category: Li X]] |
| - | [[Category: Shi, N]] | + | [[Category: Niu L]] |
| - | [[Category: Teng, M]] | + | [[Category: Shi N]] |
| - | [[Category: Gtpase-like]]
| + | [[Category: Teng M]] |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Paf1 complex]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription elongation]]
| + | |
| Structural highlights
Function
[CDC73_YEAST] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.[1] [2] [3]
Publication Abstract from PubMed
The yeast Paf1 complex (Paf1C), which is composed of the proteins Paf1, Cdc73, Ctr9, Leo1 and Rtf1, accompanies RNA polymerase II from the promoter to the 3'-end formation site of mRNA- and snoRNA-encoding genes. As one of the first identified subunits of Paf1C, yeast Cdc73 (yCdc73) takes part in many transcription-related processes, including binding to RNA polymerase II, recruitment and activation of histone-modification factors and communication with other transcriptional activators. The human homologue of yCdc73, parafibromin, has been identified as a tumour suppressor linked to breast, renal and gastric cancers. However, the functional mechanism of yCdc73 has until recently been unclear. Here, a 2.2 A resolution crystal structure of the highly conserved C-terminal region of yCdc73 is reported. It revealed that yCdc73 appears to have a GTPase-like fold. However, no GTPase activity was observed. The crystal structure of yCdc73 will shed new light on the modes of function of Cdc73 and Paf1C.
Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold.,Chen H, Shi N, Gao Y, Li X, Teng M, Niu L Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):953-9. Epub 2012 Jul 7. PMID:22868760[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shi X, Chang M, Wolf AJ, Chang CH, Frazer-Abel AA, Wade PA, Burton ZF, Jaehning JA. Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. Mol Cell Biol. 1997 Mar;17(3):1160-9. PMID:9032243
- ↑ Porter SE, Penheiter KL, Jaehning JA. Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization. Eukaryot Cell. 2005 Jan;4(1):209-20. PMID:15643076 doi:http://dx.doi.org/10.1128/EC.4.1.209-220.2005
- ↑ Sheldon KE, Mauger DM, Arndt KM. A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation. Mol Cell. 2005 Oct 28;20(2):225-36. PMID:16246725 doi:S1097-2765(05)01568-6
- ↑ Chen H, Shi N, Gao Y, Li X, Teng M, Niu L. Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold. Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):953-9. Epub 2012 Jul 7. PMID:22868760 doi:10.1107/S0907444912017325
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