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


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
05 04 2023
Historique:
received: 28 08 2022
accepted: 21 03 2023
medline: 7 4 2023
entrez: 5 4 2023
pubmed: 6 4 2023
Statut: epublish

Résumé

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.

Identifiants

pubmed: 37019967
doi: 10.1038/s41467-023-37528-3
pii: 10.1038/s41467-023-37528-3
pmc: PMC10076317
doi:

Substances chimiques

Nucleoside-Triphosphatase EC 3.6.1.15
DNA Helicases EC 3.6.4.-
RNA Helicases EC 3.6.4.13
DNA 9007-49-2

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1886

Subventions

Organisme : NCI NIH HHS
ID : P01 CA092584
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA193318
Pays : United States

Informations de copyright

© 2023. The Author(s).

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Auteurs

Junqiao Jia (J)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany.
Harvard Medical School, Department of Cell Biology, 240 Longwood Avenue, Boston, MA, 02115, USA.

Tarek Hilal (T)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany.
Freie Universität Berlin, Institute of Chemistry and Biochemistry, Research Center of Electron Microscopy, Fabeckstr. 36a, D-14195, Berlin, Germany.

Katherine E Bohnsack (KE)

Universitätsmedizin Göttingen, Department of Molecular Biology, Humboldallee 23, D-37073, Göttingen, Germany.

Aleksandar Chernev (A)

Max-Planck-Institut für Multidisziplinäre Naturwissenschaften, Bioanalytical Mass Spectrometry, Am Fassberg 11, D-37077, Göttingen, Germany.

Ning Tsao (N)

Washington University School of Medicine, Department of Pathology & Immunology and Center for Genome Integrity, 660 S. Euclid Ave, St. Louis, MO, 63110, USA.

Juliane Bethmann (J)

Max-Planck-Institut für Multidisziplinäre Naturwissenschaften, Bioanalytical Mass Spectrometry, Am Fassberg 11, D-37077, Göttingen, Germany.
Universitätsmedizin Göttingen, Institut für Klinische Chemie, Bioanalytik, Robert-Koch-Straße 40, D-35075, Göttingen, Germany.

Aruna Arumugam (A)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany.

Lane Parmely (L)

Washington University School of Medicine, Department of Pathology & Immunology and Center for Genome Integrity, 660 S. Euclid Ave, St. Louis, MO, 63110, USA.

Nicole Holton (N)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany.

Bernhard Loll (B)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany.

Nima Mosammaparast (N)

Washington University School of Medicine, Department of Pathology & Immunology and Center for Genome Integrity, 660 S. Euclid Ave, St. Louis, MO, 63110, USA.

Markus T Bohnsack (MT)

Universitätsmedizin Göttingen, Department of Molecular Biology, Humboldallee 23, D-37073, Göttingen, Germany.
Georg-August-Universität, Göttingen Center for Molecular Biosciences, Justus-von-Liebig-Weg 11, D-37077, Göttingen, Germany.
Max-Planck-Institut für Multidisziplinäre Naturwissenschaften, Am Fassberg 11, D-37077, Göttingen, Germany.

Henning Urlaub (H)

Max-Planck-Institut für Multidisziplinäre Naturwissenschaften, Bioanalytical Mass Spectrometry, Am Fassberg 11, D-37077, Göttingen, Germany.
Universitätsmedizin Göttingen, Institut für Klinische Chemie, Bioanalytik, Robert-Koch-Straße 40, D-35075, Göttingen, Germany.

Markus C Wahl (MC)

Freie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustr. 6, D-14195, Berlin, Germany. markus.wahl@fu-berlin.de.
Helmholtz-Zentrum Berlin für Materialien und Energie, Macromolecular Crystallography, Albert-Einstein-Str. 15, D-12489, Berlin, Germany. markus.wahl@fu-berlin.de.

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Classifications MeSH