Evaluation of the enzymatic properties of DNA (cytosine-5)-methyltransferase M.ApeKI from archaea in the presence of metal ions.

Aeropyrum pernix K1 Archaea DNA methyltransferase Metal ions Thermostable enzyme

Journal

Bioscience, biotechnology, and biochemistry
ISSN: 1347-6947
Titre abrégé: Biosci Biotechnol Biochem
Pays: England
ID NLM: 9205717

Informations de publication

Date de publication:
31 Jul 2024
Historique:
medline: 1 8 2024
pubmed: 1 8 2024
entrez: 31 7 2024
Statut: aheadofprint

Résumé

We previously identified M.ApeKI from Aeropyum pernix K1 as a highly thermostable DNA (cytosine-5)-methyltransferase. M.ApeKI uses the type II restriction-modification system (R-M system), among the best-studied R-M systems. Although endonucleases generally utilize Mg (II) as a cofactor, several reports have shown that MTases exhibit different reactions in the presence of metal ions. This study aim was to evaluate the enzymatic properties of DNA (cytosine-5)-methyltransferase M.ApeKI from archaea in the presence of metal ions. We evaluated the influence of metal ions on the catalytic activity and DNA binding of M.ApeKI. The catalytic activity was inhibited by Cu (II), Mg (II), Mn (II), and Zn (II), each at 5 mM. DNA binding was more strongly inhibited by 5 mM Cu (II) and 10 mM Zn (II). To our knowledge, this is the first report showing that DNA binding of typeII MTase is inhibited by metal ions.

Identifiants

DOI: 10.1093/bbb/zbae106 PMID: 39085041
pubmed: 39085041
pii: 7725074
doi: 10.1093/bbb/zbae106
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© The Author(s) 2024. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.

Auteurs

Mao Hayashi (M)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Yoshinari Wada (Y)

Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Akira Yamamura (A)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.
Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Hideki Inoue (H)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.
Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Naoya Yamashita (N)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.
Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Shigetoshi Ichimura (S)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.
Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Yasuhiro Iida (Y)

Department of Applied Chemistry and Bioscience, Graduate School of Engineering, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.
Department of Applied Bioscience, Faculty of Applied Bioscience, Kanagawa Institute of Technology, Kanagawa, Japan. 1030 Shimo-ogino, Atsugi, Kanagawa, Japan.

Classifications MeSH