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Journal Article

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

MPS-Authors
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Schuller,  Sandra K.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schuller,  Jan M.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Prabu,  J. Rajan
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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

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

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

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

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Fulltext (public)

elife-61467-v2.pdf
(Publisher version), 4MB

Supplementary Material (public)

elife-61467-figures-v2.pdf
(Supplementary material), 11MB

Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0007-AD09-D
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.