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PMID: 6278447 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Purification and characterization of two new modification methylases: MClaI from Caryophanon latum L and MTaqI from Thermus aquaticus YTI.

Nucleic acids research ·Vol. 9 ·No. 24 ·1981-12-21 ·Pages 6795-804

McClelland M

Abstract

A method for detecting Type II modification methylases and determining their methylation site by assaying the ability of methylated DNA to be cleaved by heterologous restriction enzymes is described and applied to the isolation of the restriction modification methylases from Thermus thermophilus HB8, Thermus aquaticus YTI and Caryophanon latum L. M.TaqI is shown to have a methylation specificity identical to M.ThI (TCGmeA). M.ClaI methylates at adenine and protects a subset of TthI sites indicating that it methylates the sequence ATCGmeAT. Methylation by M.ThI also protects against cleavage by SalI, XhoI and at some HindII, AccI and MboI sites.

MeSH Terms
Adenine Bacteria/enzymology Base Sequence DNA Restriction Enzymes Methyltransferases/isolation & purification Site-Specific DNA-Methyltransferase (Adenine-Specific) Substrate Specificity Thermus/enzymology
Chemicals
DNA modification methylase MClaI DNA modification methylase MTaqI Methyltransferases Site-Specific DNA-Methyltransferase (Adenine-Specific) DNA Restriction Enzymes Adenine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
McClelland M
References (14)
14 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1981-12-21
Pages
6795-804
Language
English
Region
England
NLM ID
0411011
PMCID
PMC327642
Subset
IM
Grants
NCRR NIH HHS · RF 10-21-RR093-009 · United States
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