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DNA methylases for site-selective inhibition of type IIS restriction enzyme activity

Abstract:

DNA methylases of the restriction-modifications (R-M) systems are promising enzymes for the development of novel molecular and synthetic biology tools. Their use in vitro enables the deployment of independent and controlled catalytic reactions. This work aimed to produce recombinant DNA methylases belonging to the R-M systems, capable of in vitro inhibition of the type IIS restriction enzymes BsaI, BpiI, or LguI. Non-switchable methylases are those whose recognition sequences fully overlap the recognition sequences of their associated endonuclease. In switch methylases, the methylase and endonuclease recognition sequences only partially overlap, allowing sequence engineering to alter methylation without altering restriction. In this work, ten methylases from type I and II R-M systems were selected for cloning and expression in E. coli strains tolerant to methylation. Isopropyl β-D-1-thiogalactopyranoside (IPTG) concentrations and post-induction temperatures were tested to optimize the soluble methylases expression, which was achieved with 0.5 mM IPTG at 20 °C. The C-terminal His6-Tag versions showed better expression than the N-terminal tagged versions. DNA methylation was analyzed using purified methylases and custom test plasmids which, after the methylation reactions, were digested using the corresponding associated type IIS endonuclease. The non-switchable methylases M2.Eco31I, M2.BsaI, M2.HpyAII, and M1.MboII along with the switch methylases M.Osp807II and M2.NmeMC58II showed the best activity for site-selective inhibition of type IIS restriction enzyme activity. This work demonstrates that our recombinant methylases were able to block the activity of type IIS endonucleases in vitro, allowing them to be developed as valuable tools in synthetic biology and DNA assembly techniques.

Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1007/s00253-024-13015-7

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Oxford college:
Queen's College
Role:
Author
ORCID:
0000-0001-9962-3248


Publisher:
Springer
Journal:
Applied Microbiology and Biotechnology More from this journal
Volume:
108
Issue:
1
Article number:
174
Publication date:
2024-01-25
Acceptance date:
2024-01-14
DOI:
EISSN:
1432-0614
ISSN:
0175-7598


Language:
English
Keywords:
Pubs id:
1606502
Local pid:
pubs:1606502
Deposit date:
2024-01-25

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