7dth: Difference between revisions
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==Solution structure of RPB6, common subunit of RNA polymerases I, II, and III== | ==Solution structure of RPB6, common subunit of RNA polymerases I, II, and III== | ||
<StructureSection load='7dth' size='340' side='right'caption='[[7dth]]' scene=''> | <StructureSection load='7dth' size='340' side='right'caption='[[7dth]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[7dth]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DTH FirstGlance]. <br> | ||
</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=7dth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dth OCA], [https://pdbe.org/7dth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dth RCSB], [https://www.ebi.ac.uk/pdbsum/7dth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dth ProSAT]</span></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=7dth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dth OCA], [https://pdbe.org/7dth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dth RCSB], [https://www.ebi.ac.uk/pdbsum/7dth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dth ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/RPAB2_HUMAN RPAB2_HUMAN]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and togther with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).<ref>PMID:9852112</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, three RNA polymerases (RNAPs) play essential roles in the synthesis of various types of RNA: namely, RNAPI for rRNA; RNAPII for mRNA and most snRNAs; and RNAPIII for tRNA and other small RNAs. All three RNAPs possess a short flexible tail derived from their common subunit RPB6. However, the function of this shared N-terminal tail (NTT) is not clear. Here we show that NTT interacts with the PH domain (PH-D) of the p62 subunit of the general transcription/repair factor TFIIH, and present the structures of RPB6 unbound and bound to PH-D by nuclear magnetic resonance (NMR). Using available cryo-EM structures, we modelled the activated elongation complex of RNAPII bound to TFIIH. We also provide evidence that the recruitment of TFIIH to transcription sites through the p62-RPB6 interaction is a common mechanism for transcription-coupled nucleotide excision repair (TC-NER) of RNAPI- and RNAPII-transcribed genes. Moreover, point mutations in the RPB6 NTT cause a significant reduction in transcription of RNAPI-, RNAPII- and RNAPIII-transcribed genes. These and other results show that the p62-RPB6 interaction plays multiple roles in transcription, TC-NER, and cell proliferation, suggesting that TFIIH is engaged in all RNAP systems. | |||
Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.,Okuda M, Suwa T, Suzuki H, Yamaguchi Y, Nishimura Y Nucleic Acids Res. 2022 Jan 11;50(1):1-16. doi: 10.1093/nar/gkab612. PMID:34268577<ref>PMID:34268577</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7dth" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Nishimura Y]] | [[Category: Nishimura, Y]] | ||
[[Category: Okuda M]] | [[Category: Okuda, M]] | ||
[[Category: Nuclear protein]] | |||
[[Category: Rna polymerase]] | |||
Revision as of 07:57, 3 August 2022
Solution structure of RPB6, common subunit of RNA polymerases I, II, and IIISolution structure of RPB6, common subunit of RNA polymerases I, II, and III
Structural highlights
Function[RPAB2_HUMAN] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and togther with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).[1] Publication Abstract from PubMedIn eukaryotes, three RNA polymerases (RNAPs) play essential roles in the synthesis of various types of RNA: namely, RNAPI for rRNA; RNAPII for mRNA and most snRNAs; and RNAPIII for tRNA and other small RNAs. All three RNAPs possess a short flexible tail derived from their common subunit RPB6. However, the function of this shared N-terminal tail (NTT) is not clear. Here we show that NTT interacts with the PH domain (PH-D) of the p62 subunit of the general transcription/repair factor TFIIH, and present the structures of RPB6 unbound and bound to PH-D by nuclear magnetic resonance (NMR). Using available cryo-EM structures, we modelled the activated elongation complex of RNAPII bound to TFIIH. We also provide evidence that the recruitment of TFIIH to transcription sites through the p62-RPB6 interaction is a common mechanism for transcription-coupled nucleotide excision repair (TC-NER) of RNAPI- and RNAPII-transcribed genes. Moreover, point mutations in the RPB6 NTT cause a significant reduction in transcription of RNAPI-, RNAPII- and RNAPIII-transcribed genes. These and other results show that the p62-RPB6 interaction plays multiple roles in transcription, TC-NER, and cell proliferation, suggesting that TFIIH is engaged in all RNAP systems. Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.,Okuda M, Suwa T, Suzuki H, Yamaguchi Y, Nishimura Y Nucleic Acids Res. 2022 Jan 11;50(1):1-16. doi: 10.1093/nar/gkab612. PMID:34268577[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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