English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family

MPS-Authors
/persons/resource/persons209024

Leonaite,  Bronislava
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77713

Basquin,  Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77784

Bonneau,  Fabien
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77867

Conti,  Elena
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

1590.full.pdf
(Publisher version), 4MB

Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-DE83-9
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.