Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.
ATPase
RadA recombinase
RecA family recombinases
Saccharolobus solfataricus
Walker box mutants
archaea
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
27 02 2023
27 02 2023
Historique:
received:
25
08
2022
revised:
20
12
2022
accepted:
03
01
2023
pubmed:
6
1
2023
medline:
25
2
2023
entrez:
5
1
2023
Statut:
ppublish
Résumé
Central to the universal process of recombination, RecA family proteins form nucleoprotein filaments to catalyze production of heteroduplex DNA between substrate ssDNAs and template dsDNAs. ATP binding assists the filament in assuming the necessary conformation for forming heteroduplex DNA, but hydrolysis is not required. ATP hydrolysis has two identified roles which are not universally conserved: promotion of filament dissociation and enhancing flexibility of the filament. In this work, we examine ATP utilization of the RecA family recombinase SsoRadA from Saccharolobus solfataricus to determine its function in recombinase-mediated heteroduplex DNA formation. Wild-type SsoRadA protein and two ATPase mutant proteins were evaluated for the effects of three divalent metal cofactors. We found that unlike other archaeal RadA proteins, SsoRadA-mediated strand exchange is not enhanced by Ca2+. Instead, the S. solfataricus recombinase can utilize Mn2+ to stimulate strand invasion and reduce ADP-binding stability. Additionally, reduction of SsoRadA ATPase activity by Walker Box mutation or cofactor alteration resulted in a loss of large, complete strand exchange products. Depletion of ADP was found to improve initial strand invasion but also led to a similar loss of large strand exchange events. Our results indicate that overall, SsoRadA is distinct in its use of divalent cofactors but its activity with Mn2+ shows similarity to human RAD51 protein with Ca2+.
Identifiants
pubmed: 36601994
pii: 232405
doi: 10.1042/BSR20221807
pmc: PMC9950535
pii:
doi:
Substances chimiques
Calcium
SY7Q814VUP
Nucleic Acid Heteroduplexes
0
Rec A Recombinases
EC 2.7.7.-
Recombinases
0
Adenosine Triphosphatases
EC 3.6.1.-
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM008336
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM083864
Pays : United States
Informations de copyright
© 2023 The Author(s).
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