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Updated: Nov 30, 2025

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
Published on: October 23, 2014
Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex
Sandra K Schuller1, Jan M Schuller1, J Rajan Prabu1
1Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
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 Å resolution structure of Saccharomyces cerevisiae 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.
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