Bloom Syndrome Helicase Compresses Single-Stranded DNA into Phase-Separated Condensates.
Biomolecular Condensate
Bloom Syndrome Protein
Helicase
Phase Separation
Single-Molecule Studies
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
26 09 2022
26 09 2022
Historique:
received:
28
06
2022
pubmed:
4
8
2022
medline:
23
9
2022
entrez:
3
8
2022
Statut:
ppublish
Résumé
Bloom syndrome protein (BLM) is a conserved RecQ family helicase involved in the maintenance of genome stability. BLM has been widely recognized as a genome "caretaker" that processes structured DNA. In contrast, our knowledge of how BLM behaves on single-stranded (ss) DNA is still limited. Here, we demonstrate that BLM possesses the intrinsic ability for phase separation and can co-phase separate with ssDNA to form dynamically arrested protein/ssDNA co-condensates. The introduction of ATP potentiates the capability of BLM to condense on ssDNA, which further promotes the compression of ssDNA against a resistive force of up to 60 piconewtons. Moreover, BLM is also capable of condensing replication protein A (RPA)- or RAD51-coated ssDNA, before which it generates naked ssDNA by dismantling these ssDNA-binding proteins. Overall, our findings identify an unexpected characteristic of a DNA helicase and provide a new angle of protein/ssDNA co-condensation for understanding the genomic instability caused by BLM overexpression under diseased conditions.
Identifiants
pubmed: 35922882
doi: 10.1002/anie.202209463
doi:
Substances chimiques
DNA, Single-Stranded
0
Replication Protein A
0
Adenosine Triphosphate
8L70Q75FXE
DNA
9007-49-2
Bloom syndrome protein
EC 3.6.1.-
RecQ Helicases
EC 3.6.4.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202209463Informations de copyright
© 2022 Wiley-VCH GmbH.
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