| Structural highlights
5mzn is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.787Å |
| Ligands: | ADP, EDO, GOL, MG, PEG |
| 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 superfamily 1B (SF1B) helicase Sen1 is an essential protein that plays a key role in the termination of non-coding transcription in yeast. Here, we identified the ~90 kDa helicase core of Saccharomyces cerevisiae Sen1 as sufficient for transcription termination in vitro and determined the corresponding structure at 1.8 A resolution. In addition to the catalytic and auxiliary subdomains characteristic of the SF1B family, Sen1 has a distinct and evolutionarily conserved structural feature that "braces" the helicase core. Comparative structural analyses indicate that the "brace" is essential in shaping a favorable conformation for RNA binding and unwinding. We also show that subdomain 1C (the "prong") is an essential element for 5'-3' unwinding and for Sen1-mediated transcription termination in vitro Finally, yeast Sen1 mutant proteins mimicking the disease forms of the human orthologue, senataxin, show lower capacity of RNA unwinding and impairment of transcription termination in vitro The combined biochemical and structural data thus provide a molecular model for the specificity of Sen1 in transcription termination and more generally for the unwinding mechanism of 5'-3' helicases.
Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family.,Leonaite B, Han Z, Basquin J, Bonneau F, Libri D, Porrua O, Conti E EMBO J. 2017 Apr 13. pii: e201696174. doi: 10.15252/embj.201696174. PMID:28408439[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:https://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:https://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:https://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
- ↑ Leonaite B, Han Z, Basquin J, Bonneau F, Libri D, Porrua O, Conti E. Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family. EMBO J. 2017 Apr 13. pii: e201696174. doi: 10.15252/embj.201696174. PMID:28408439 doi:https://dx.doi.org/10.15252/embj.201696174
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