8him: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8him]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_oleracea Brassica oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HIM FirstGlance]. <br>
<table><tr><td colspan='2'>[[8him]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_oleracea Brassica oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HIM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=8him FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8him OCA], [https://pdbe.org/8him PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8him RCSB], [https://www.ebi.ac.uk/pdbsum/8him PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8him 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=8him FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8him OCA], [https://pdbe.org/8him PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8him RCSB], [https://www.ebi.ac.uk/pdbsum/8him PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8him ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A0D2ZPP3_BRAOL A0A0D2ZPP3_BRAOL]  
[https://www.uniprot.org/uniprot/A0A0D3D418_BRAOL A0A0D3D418_BRAOL]  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
In addition to the conserved RNA polymerases (Pols) I-III in eukaryotes, two atypical polymerases, Pols IV and V, specifically produce non-coding RNA in the RNA-directed DNA methylation (RdDM) pathway in plants. Here, we report on the structures of cauliflower Pol V in the free and elongation conformations. A conserved tyrosine residue of NRPE2 stacks with a dsDNA branch of the transcription bubble to potentially attenuate elongation by inducing transcription stalling. The non-template DNA strand is captured by NRPE2 to enhance backtracking, thereby increasing 3'-5' cleavage which likely underpins Pol V's high fidelity. The structures also illuminate the mechanism of Pol V transcription stalling and enhanced backtracking which may be important for Pol V's retention on chromatin to serve its function in tethering downstream factors for RdDM.
In addition to the conserved RNA polymerases I to III (Pols I to III) in eukaryotes, two atypical polymerases, Pols IV and V, specifically produce noncoding RNA in the RNA-directed DNA methylation pathway in plants. Here, we report on the structures of cauliflower Pol V in the free and elongation conformations. A conserved tyrosine residue of NRPE2 stacks with a double-stranded DNA branch of the transcription bubble to potentially attenuate elongation by inducing transcription stalling. The nontemplate DNA strand is captured by NRPE2 to enhance backtracking, thereby increasing 3'-5' cleavage, which likely underpins Pol V's high fidelity. The structures also illuminate the mechanism of Pol V transcription stalling and enhanced backtracking, which may be important for Pol V's retention on chromatin to serve its function in tethering downstream factors for RNA-directed DNA methylation.


Structure and mechanism of the plant RNA polymerase V.,Xie G, Du X, Hu H, Li S, Cao X, Jacobsen SE, Du J Science. 2023 Mar 9:eadf8231. doi: 10.1126/science.adf8231. PMID:36893216<ref>PMID:36893216</ref>
Structure and mechanism of the plant RNA polymerase V.,Xie G, Du X, Hu H, Li S, Cao X, Jacobsen SE, Du J Science. 2023 Mar 24;379(6638):1209-1213. doi: 10.1126/science.adf8231. Epub 2023 , Mar 9. PMID:36893216<ref>PMID:36893216</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 8him" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 8him" style="background-color:#fffaf0;"></div>
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>

Latest revision as of 07:38, 3 July 2024

A cryo-EM structure of B. oleracea RNA polymerase V elongation complex at 2.73 Angstrom

8him, resolution 2.80Å

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