The N-terminal domain of the Agrobacterium tumefaciens telomere resolvase, TelA, regulates its DNA cleavage and rejoining activities.

bacterial telomeres divalent metal ions enzyme autoinhibition genome linearity telomere fusion telomere recombination telomere resolution

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
05 2022
Historique:
received: 28 01 2022
revised: 08 04 2022
accepted: 09 04 2022
pubmed: 22 4 2022
medline: 7 6 2022
entrez: 21 4 2022
Statut: ppublish

Résumé

Linear replicons can be found in a minority of prokaryotic organisms, including Borrelia species and Agrobacterium tumefaciens. The problem with replicating the lagging strand end of linear DNAs is circumvented in these organisms by the presence of covalently closed DNA hairpin telomeres at the DNA termini. Telomere resolvases are enzymes responsible for generating these hairpin telomeres from a dimeric replication intermediate through a two-step DNA cleavage and rejoining reaction referred to as telomere resolution. It was previously shown that the agrobacterial telomere resolvase, TelA, possesses ssDNA annealing activity in addition to telomere resolution activity. The annealing activity derives, chiefly, from the N-terminal domain. This domain is dispensable for telomere resolution. In this study, we used activity analyses of an N-terminal domain deletion mutant, domain add back experiments, and protein-protein interaction studies and we report that the N-terminal domain of TelA is involved in inhibitory interactions with the remainder of TelA that are relieved by the binding of divalent metal ions. We also found that the regulation of telomere resolution by the N-terminal domain of TelA extends to suppression of inappropriate enzymatic activity, including hairpin telomere fusion (reaction reversal) and recombination between replicated telomeres to form a Holliday junction.

Identifiants

pubmed: 35447111
pii: S0021-9258(22)00391-X
doi: 10.1016/j.jbc.2022.101951
pmc: PMC9111995
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Recombinases 0
DNA 9007-49-2

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

101951

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Siobhan L McGrath (SL)

Department of Biochemistry, Microbiology & Immunology, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.

Shu Hui Huang (SH)

Department of Biochemistry, Microbiology & Immunology, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.

Kerri Kobryn (K)

Department of Biochemistry, Microbiology & Immunology, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan, Canada. Electronic address: kerri.kobryn@usask.ca.

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Classifications MeSH