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-Structure paper
Title | Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex. |
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Journal, issue, pages | Elife, Vol. 9, Year 2020 |
Publish date | Nov 16, 2020 |
Authors | Sandra K Schuller / Jan M Schuller / J Rajan Prabu / Marc Baumgärtner / Fabien Bonneau / Jérôme Basquin / Elena Conti / |
PubMed 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 ...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 Å resolution structure of THO-Sub2 by cryo-electron microscopy. THO subunits Tho2 and Hpr1 intertwine to form a platform that is bound by Mft1, Thp2, and Tex1. 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. |
External links | Elife / PubMed:33191913 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.4 - 4.5 Å |
Structure data | EMDB-11859, PDB-7apx: EMDB-11871, PDB-7aqo: |
Source |
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Keywords | RNA BINDING PROTEIN / yeast THO complex S. cerevisiae THO-Sub2 the transcription-export (TREX) complex |