8ran

From Proteopedia

(Difference between revisions)

Current revision

Structure of Sen1-RNA complex

Structural highlights

8ran is a 2 chain structure with sequence from Human immunodeficiency virus 2 and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.25Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SEN1_YEAST ATP-dependent 5'->3' DNA/RNA helicase required for the expression and maturation of diverse classes of non-protein-coding RNAs like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar (snoRNA) RNAs. Directs RNA polymerase II transcription termination on snoRNAs as well as on several short protein-coding genes. May also play a role in transcription-coupled nucleotide excision repair.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of polyadenylation-independent Pol II termination mediated by the yeast Sen1 helicase. Cryo-electron microscopy structures of two pretermination intermediates show that Sen1 binds to Pol II and uses its adenosine triphosphatase activity to pull on exiting RNA in the 5' direction. This is predicted to push Pol II forward, induce an unstable hypertranslocated state and destabilize the transcription bubble, thereby facilitating termination. This mechanism of transcription termination may be widely used because it is conceptually conserved in the bacterial transcription system.

Mechanism of polyadenylation-independent RNA polymerase II termination.,Rengachari S, Hainthaler T, Oberthuer C, Lidschreiber M, Cramer P Nat Struct Mol Biol. 2024 Oct 18. doi: 10.1038/s41594-024-01409-0. PMID:39424994^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Steinmetz EJ, Conrad NK, Brow DA, Corden JL. RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature. 2001 Sep 20;413(6853):327-31. PMID:11565036 doi:http://dx.doi.org/10.1038/35095090
↑ Ursic D, Chinchilla K, Finkel JS, Culbertson MR. Multiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing. Nucleic Acids Res. 2004 Apr 30;32(8):2441-52. Print 2004. PMID:15121901 doi:http://dx.doi.org/10.1093/nar/gkh561
↑ Steinmetz EJ, Warren CL, Kuehner JN, Panbehi B, Ansari AZ, Brow DA. Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol Cell. 2006 Dec 8;24(5):735-46. PMID:17157256 doi:http://dx.doi.org/10.1016/j.molcel.2006.10.023
↑ Steinmetz EJ, Brow DA. Repression of gene expression by an exogenous sequence element acting in concert with a heterogeneous nuclear ribonucleoprotein-like protein, Nrd1, and the putative helicase Sen1. Mol Cell Biol. 1996 Dec;16(12):6993-7003. PMID:8943355
↑ Ursic D, Himmel KL, Gurley KA, Webb F, Culbertson MR. The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res. 1997 Dec 1;25(23):4778-85. PMID:9365256
↑ Rasmussen TP, Culbertson MR. The putative nucleic acid helicase Sen1p is required for formation and stability of termini and for maximal rates of synthesis and levels of accumulation of small nucleolar RNAs in Saccharomyces cerevisiae. Mol Cell Biol. 1998 Dec;18(12):6885-96. PMID:9819377
↑ Rengachari S, Hainthaler T, Oberthuer C, Lidschreiber M, Cramer P. Mechanism of polyadenylation-independent RNA polymerase II termination. Nat Struct Mol Biol. 2024 Oct 18. PMID:39424994 doi:10.1038/s41594-024-01409-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8ran"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8ran is ON HOLD  until Paper Publication
+==Structure of Sen1-RNA complex==
+<StructureSection load='8ran' size='340' side='right'caption='[[8ran]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8ran]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_2 Human immunodeficiency virus 2] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RAN 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]] 3.25&#8491;</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=8ran FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ran OCA], [https://pdbe.org/8ran PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ran RCSB], [https://www.ebi.ac.uk/pdbsum/8ran PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ran ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SEN1_YEAST SEN1_YEAST] ATP-dependent 5'->3' DNA/RNA helicase required for the expression and maturation of diverse classes of non-protein-coding RNAs like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar (snoRNA) RNAs. Directs RNA polymerase II transcription termination on snoRNAs as well as on several short protein-coding genes. May also play a role in transcription-coupled nucleotide excision repair.<ref>PMID:11565036</ref> <ref>PMID:15121901</ref> <ref>PMID:17157256</ref> <ref>PMID:8943355</ref> <ref>PMID:9365256</ref> <ref>PMID:9819377</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of polyadenylation-independent Pol II termination mediated by the yeast Sen1 helicase. Cryo-electron microscopy structures of two pretermination intermediates show that Sen1 binds to Pol II and uses its adenosine triphosphatase activity to pull on exiting RNA in the 5' direction. This is predicted to push Pol II forward, induce an unstable hypertranslocated state and destabilize the transcription bubble, thereby facilitating termination. This mechanism of transcription termination may be widely used because it is conceptually conserved in the bacterial transcription system.
-Authors: Rengachari, S., Lidscreiber, M., Cramer, P.
+Mechanism of polyadenylation-independent RNA polymerase II termination.,Rengachari S, Hainthaler T, Oberthuer C, Lidschreiber M, Cramer P Nat Struct Mol Biol. 2024 Oct 18. doi: 10.1038/s41594-024-01409-0. PMID:39424994<ref>PMID:39424994</ref>
-Description: Structure of Sen1-RNA complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Cramer, P]]
+<div class="pdbe-citations 8ran" style="background-color:#fffaf0;"></div>
-[[Category: Rengachari, S]]
+== References ==
-[[Category: Lidscreiber, M]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Human immunodeficiency virus 2]]
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae]]
+[[Category: Cramer P]]
+[[Category: Lidscreiber M]]
+[[Category: Rengachari S]]

8ran

From Proteopedia

Current revision

Structure of Sen1-RNA complex

Structural highlights

Function

Publication Abstract from PubMed

References

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