Multivalent forms of the ribonuclease H1 hybrid binding domain are high-affinity binders of RNA-DNA hybrids.
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
revised:
18
10
2022
received:
05
05
2022
accepted:
22
10
2022
pubmed:
30
11
2022
medline:
16
2
2023
entrez:
29
11
2022
Statut:
ppublish
Résumé
The hybrid binding domain (HBD) is a conserved fold present in ribonucleases H1 that selectively recognizes RNA-DNA hybrids, which are structures present in cellular R-loops and participate in diverse biological processes. We engineered multivalent HBD proteins to create high-affinity hybrid binders. Using EMSA- and SPR-based analyses, we showed that the triple-HBD protein exhibits a ~ 22 000-fold increase in hybrid affinity (K
Identifiants
pubmed: 36443824
doi: 10.1002/1873-3468.14541
doi:
Substances chimiques
RNA
63231-63-0
ribonuclease HI
EC 3.1.26.4
DNA
9007-49-2
Ribonuclease H
EC 3.1.26.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
472-482Informations de copyright
© 2022 Federation of European Biochemical Societies.
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