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  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., et al. (2017). Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family. EMBO Journal, 36(11), 1590-1604. doi:10.15252/embj.201696174.

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 Creators:
Leonaite, Bronislava1, Author              
Han, Zhong2, Author
Basquin, Jerome1, Author              
Bonneau, Fabien1, Author              
Libri, Domenico2, Author
Porrua, Odil2, Author
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: RNA-POLYMERASE-II; SACCHAROMYCES-CEREVISIAE SEN1; TRANSCRIPTION TERMINATION; BUDDING YEAST; HUMAN UPF1; HUMAN SENATAXIN; MOLECULAR-BASIS; RIBOSOMAL-RNA; DNA HELICASE; PROTEINBiochemistry & Molecular Biology; Cell Biology; non-coding transcription; RNA helicases; transcription termination;
 Abstract: 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 similar to 90 kDa helicase core of Saccharomyces cerevisiae Sen1 as sufficient for transcription termination in vitro and determined the corresponding structure at 1.8 angstrom 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.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000402532200011
DOI: 10.15252/embj.201696174
 Degree: -

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Project name : ERC Advanced Investigator Grant 294371
Grant ID : 294371
Funding program : -
Funding organization : European Commission (EC)

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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 36 (11) Sequence Number: - Start / End Page: 1590 - 1604 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061