7ast: Difference between revisions
New page: '''Unreleased structure''' The entry 7ast is ON HOLD Authors: Ramsay, E.P., Abascal-Palacios, G., Daiss, J.L., King, H., Gouge, J., Pilsl, M., Beuron, F., Morris, E., Gunkel, P., Engel,... |
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The entry | ==Apo Human RNA Polymerase III== | ||
<StructureSection load='7ast' size='340' side='right'caption='[[7ast]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ast]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AST FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=7ast FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ast OCA], [https://pdbe.org/7ast PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ast RCSB], [https://www.ebi.ac.uk/pdbsum/7ast PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ast ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/RPC10_HUMAN RPC10_HUMAN] The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RPC10_HUMAN RPC10_HUMAN] Core component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:30584594, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218). Can mediate Pol I proofreading of the nascent RNA transcript. Anchors into the Pol III active site to constantly monitor transcription fidelity, cleaves mis-incorporated 5'-ribonucleotides and restarts the transcription process. Once Pol III reaches the poly(dT) termination signal, can induce Pol III clamp opening and transcription termination (By similarity) (PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218). Pol III plays an important role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway (PubMed:19609254, PubMed:19631370).[UniProtKB:Q04307]<ref>PMID:19609254</ref> <ref>PMID:19631370</ref> <ref>PMID:20413673</ref> <ref>PMID:30584594</ref> <ref>PMID:33335104</ref> <ref>PMID:33558764</ref> <ref>PMID:33558766</ref> <ref>PMID:33674783</ref> <ref>PMID:34675218</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, RNA Polymerase (Pol) III is specialized for the transcription of tRNAs and other short, untranslated RNAs. Pol III is a determinant of cellular growth and lifespan across eukaryotes. Upregulation of Pol III transcription is observed in cancer and causative Pol III mutations have been described in neurodevelopmental disorders and hypersensitivity to viral infection. Here, we report a cryo-EM reconstruction at 4.0 A of human Pol III, allowing mapping and rationalization of reported genetic mutations. Mutations causing neurodevelopmental defects cluster in hotspots affecting Pol III stability and/or biogenesis, whereas mutations affecting viral sensing are located in proximity to DNA binding regions, suggesting an impairment of Pol III cytosolic viral DNA-sensing. Integrating x-ray crystallography and SAXS, we also describe the structure of the higher eukaryote specific RPC5 C-terminal extension. Surprisingly, experiments in living cells highlight a role for this module in the assembly and stability of human Pol III. | |||
Structure of human RNA polymerase III.,Ramsay EP, Abascal-Palacios G, Daiss JL, King H, Gouge J, Pilsl M, Beuron F, Morris E, Gunkel P, Engel C, Vannini A Nat Commun. 2020 Dec 17;11(1):6409. doi: 10.1038/s41467-020-20262-5. PMID:33335104<ref>PMID:33335104</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ast" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Gunkel | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Abascal-Palacios G]] | ||
[[Category: Beuron F]] | |||
[[Category: Daiss JL]] | |||
[[Category: Engel C]] | |||
[[Category: Gouge J]] | |||
[[Category: Gunkel P]] | |||
[[Category: King H]] | |||
[[Category: Morris E]] | |||
[[Category: Pilsl M]] | |||
[[Category: Ramsay EP]] | |||
[[Category: Vannini A]] | |||