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  Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex

Schuller, S. K., Schuller, J. M., Prabu, J. R., Baumgärtner, M., Bonneau, F., Basquin, J., et al. (2020). Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex. eLife, 9: e61467. doi:10.7554/eLife.61467.

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 Creators:
Schuller, Sandra K.1, Author              
Schuller, Jan M.1, Author              
Prabu, J. Rajan1, Author              
Baumgärtner, Marc1, Author              
Bonneau, Fabien1, Author              
Basquin, Jerome1, Author              
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: MESSENGER-RNA EXPORT; TRANSCRIPTION ELONGATION; SACCHAROMYCES-CEREVISIAE; GENE-EXPRESSION; MRNP FORMATION; THO COMPLEX; R-LOOPS; PROTEIN; HELICASE; TREXLife Sciences & Biomedicine - Other Topics;
 Abstract: The yeast THO complex is recruited to active genes and interacts with the RNA-dependent ATPase Sub2 to facilitate the formation of mature export-competent messenger ribonucleoprotein particles and to prevent the co-transcriptional formation of RNA:DNA-hybrid-containing structures. How THO-containing complexes function at the mechanistic level is unclear. Here, we elucidated a 3.4 angstrom resolution structure of Saccharomyces cerevisiae THO-Sub2 by cryoelectron microscopy. THO subunits Tho2 and Hpr1 intertwine to form a platform that is bound by Mft1, Thp2, and Text. The resulting complex homodimerizes in an asymmetric fashion, with a Sub2 molecule attached to each protomer. The homodimerization interfaces serve as a fulcrum for a seesaw-like movement concomitant with conformational changes of the Sub2 ATPase. The overall structural architecture and topology suggest the molecular mechanisms of nucleic acid remodeling during mRNA biogenesis.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 16
 Publishing info: -
 Table of Contents: We thank Daniel Bollschweiler and Tillman Schäfer at the MPIB cryo-EM facility...
 Rev. Type: -
 Identifiers: ISI: 000600161700001
DOI: 10.7554/eLife.61467
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Project name : ERC Advanced Investigator Grant EXORICO
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Funding organization : European Commission
Project name : GRK1721, SFB/TRR 237
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Funding program : -
Funding organization : German Research Foundation

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 9 Sequence Number: e61467 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X