Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.
ATPASE ACTIVITY
CALCIUM
STRAND EXCHANGE
ssoRadA
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
28 06 2023
28 06 2023
Historique:
received:
08
04
2023
revised:
13
06
2023
accepted:
14
06
2023
medline:
29
6
2023
pubmed:
19
6
2023
entrez:
19
6
2023
Statut:
ppublish
Résumé
RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.
Identifiants
pubmed: 37334574
pii: 233153
doi: 10.1042/BSR20230058
pmc: PMC10311128
pii:
doi:
Substances chimiques
DNA-Binding Proteins
0
Cations, Divalent
0
Adenosine Triphosphatases
EC 3.6.1.-
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2023 The Author(s).
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