Exploration of DNA processing features unravels novel properties of ICE conjugation in Gram-positive bacteria.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
12 08 2022
12 08 2022
Historique:
accepted:
02
07
2022
revised:
02
06
2022
received:
30
11
2021
pubmed:
19
7
2022
medline:
16
8
2022
entrez:
18
7
2022
Statut:
ppublish
Résumé
Integrative and conjugative elements (ICEs) are important drivers of horizontal gene transfer in prokaryotes. They are responsible for antimicrobial resistance spread, a major current health concern. ICEs are initially processed by relaxases that recognize the binding site of oriT sequence and nick at a conserved nic site. The ICESt3/Tn916/ICEBs1 superfamily, which is widespread among Firmicutes, encodes uncanonical relaxases belonging to a recently identified family called MOBT. This family is related to the rolling circle replication initiators of the Rep_trans family. The nic site of these MOBT relaxases is conserved but their DNA binding site is still unknown. Here, we identified the bind site of RelSt3, the MOBT relaxase from ICESt3. Unexpectedly, we found this bind site distantly located from the nic site. We revealed that the binding of the RelSt3 N-terminal HTH domain is required for efficient nicking activity. We also deciphered the role of RelSt3 in the initial and final stages of DNA processing during conjugation. Especially, we demonstrated a strand transfer activity, and the formation of covalent DNA-relaxase intermediate for a MOBT relaxase.
Identifiants
pubmed: 35849337
pii: 6645636
doi: 10.1093/nar/gkac607
pmc: PMC9371924
doi:
Substances chimiques
Bacterial Proteins
0
DNA, Bacterial
0
DNA Nucleotidyltransferases
EC 2.7.7.-
DNA relaxase
EC 2.7.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8127-8142Informations de copyright
© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.
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