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| | <StructureSection load='6o3x' size='340' side='right'caption='[[6o3x]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='6o3x' size='340' side='right'caption='[[6o3x]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o3x]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o3x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O3X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.994Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6o3w|6o3w]], [[6o3y|6o3y]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3x OCA], [http://pdbe.org/6o3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o3x RCSB], [http://www.ebi.ac.uk/pdbsum/6o3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3x 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=6o3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3x OCA], [https://pdbe.org/6o3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o3x RCSB], [https://www.ebi.ac.uk/pdbsum/6o3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NRD1_YEAST NRD1_YEAST]] Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance. [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6o3x" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6o3x" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tong, L]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Tong L]] |
| - | [[Category: Cid]] | + | [[Category: Zhang Y]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Ctd mimic]]
| + | |
| - | [[Category: Transcription]]
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| Structural highlights
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 Nrd1-Nab3-Sen1 (NNS) complex carries out the transcription termination of non-coding RNAs (ncRNAs) by RNA polymerase II (Pol II) in yeast, although the detailed interactions among its subunits remain obscure. Here we have identified three sequence motifs in Sen1 that mediate direct interactions with the Pol II CTD interaction domain (CID) of Nrd1, determined the crystal structures of these Nrd1 interaction motifs (NIMs) bound to the CID, and characterized the interactions in vitro and in yeast. Removal of all three NIMs abolishes NNS complex formation and gives rise to ncRNA termination defects.
Identification of Three Sequence Motifs in the Transcription Termination Factor Sen1 that Mediate Direct Interactions with Nrd1.,Zhang Y, Chun Y, Buratowski S, Tong L Structure. 2019 Apr 23. pii: S0969-2126(19)30127-3. doi:, 10.1016/j.str.2019.04.005. PMID:31104813[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Zhang Y, Chun Y, Buratowski S, Tong L. Identification of Three Sequence Motifs in the Transcription Termination Factor Sen1 that Mediate Direct Interactions with Nrd1. Structure. 2019 Apr 23. pii: S0969-2126(19)30127-3. doi:, 10.1016/j.str.2019.04.005. PMID:31104813 doi:http://dx.doi.org/10.1016/j.str.2019.04.005
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