7pzp
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pzp]] is a 2 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=7PZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PZP FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pzp]] is a 2 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=7PZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PZP 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=7pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pzp OCA], [https://pdbe.org/7pzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pzp RCSB], [https://www.ebi.ac.uk/pdbsum/7pzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pzp ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=7pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pzp OCA], [https://pdbe.org/7pzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pzp RCSB], [https://www.ebi.ac.uk/pdbsum/7pzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pzp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RPOM_HUMAN RPOM_HUMAN] DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates.<ref>PMID:21278163</ref> | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitochondrial genome encodes 13 components of the oxidative phosphorylation system, and altered mitochondrial transcription drives various human pathologies. A polyadenylated, non-coding RNA molecule known as 7S RNA is transcribed from a region immediately downstream of the light strand promoter in mammalian cells, and its levels change rapidly in response to physiological conditions. Here, we report that 7S RNA has a regulatory function, as it controls levels of mitochondrial transcription both in vitro and in cultured human cells. Using cryo-EM, we show that POLRMT dimerization is induced by interactions with 7S RNA. The resulting POLRMT dimer interface sequesters domains necessary for promoter recognition and unwinding, thereby preventing transcription initiation. We propose that the non-coding 7S RNA molecule is a component of a negative feedback loop that regulates mitochondrial transcription in mammalian cells. | ||
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| + | Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization.,Zhu X, Xie X, Das H, Tan BG, Shi Y, Al-Behadili A, Peter B, Motori E, Valenzuela S, Posse V, Gustafsson CM, Hallberg BM, Falkenberg M Cell. 2022 Jun 23;185(13):2309-2323.e24. doi: 10.1016/j.cell.2022.05.006. Epub , 2022 Jun 2. PMID:35662414<ref>PMID:35662414</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7pzp" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Mitochondrial DNA dependent RNA polymerase homodimer.
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