Evaluation of the enzymatic properties of DNA (cytosine-5)-methyltransferase M.ApeKI from archaea in the presence of metal ions.
Biosci Biotechnol Biochem
; 2024 Jul 31.
Article
in En
| MEDLINE
| ID: mdl-39085041
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Biosci Biotechnol Biochem
Journal subject:
BIOQUIMICA
/
BIOTECNOLOGIA
Year:
2024
Document type:
Article
Affiliation country:
Japan
Country of publication:
United kingdom