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Journal Article

Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex

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Arumugam,  Aruna       
IMPRS for Biology and Computation (Anne-Dominique Gindrat), Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Nat Comm_Jia et al_2023.pdf
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Citation

Jia, J., Hilal, T., Bohnsack, K. E., Chernev, A., Tsao, N., Bethmann, J., et al. (2023). Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex. Nature Communications, 14: 1886. doi:10.1038/s41467-023-37528-3.


Cite as: https://hdl.handle.net/21.11116/0000-000E-3CA4-6
Abstract
Activating signal co-integrator 1 complex (ASCC) subunit 3 (ASCC3) supports diverse genome maintenance and gene expression processes, and contains tandem Ski2-like NTPase/helicase cassettes crucial for these functions. Presently, the molecular mechanisms underlying ASCC3 helicase activity and regulation remain unresolved. We present cryogenic electron microscopy, DNA-protein cross-linking/mass spectrometry as well as in vitro and cellular functional analyses of the ASCC3-TRIP4 sub-module of ASCC. Unlike the related spliceosomal SNRNP200 RNA helicase, ASCC3 can thread substrates through both helicase cassettes. TRIP4 docks on ASCC3 via a zinc finger domain and stimulates the helicase by positioning an ASC-1 homology domain next to the C-terminal helicase cassette of ASCC3, likely supporting substrate engagement and assisting the DNA exit. TRIP4 binds ASCC3 mutually exclusively with the DNA/RNA dealkylase, ALKBH3, directing ASCC3 for specific processes. Our findings define ASCC3-TRIP4 as a tunable motor module of ASCC that encompasses two cooperating NTPase/helicase units functionally expanded by TRIP4.