M.Smal is an N4-methylcytosine specific DNA-methylase
Author(s) -
Saulius Klimašauskas,
Dana Steponavičiene,
Z. Manelienė,
M. Petrušyté,
Viktoras Butkus,
A. Janulaitis
Publication year - 1990
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/18.22.6607
Subject(s) - 5 methylcytosine , biology , cytosine , methyltransferase , dna , serratia marcescens , restriction enzyme , methionine , microbiology and biotechnology , endonuclease , dna methyltransferase , enzyme , biochemistry , methylation , dna methylation , escherichia coli , amino acid , gene , gene expression
An enzymatic activity rendering DNA immune to the action of the Smal restriction endonuclease in the presence of S-adenosyl-L-methionine has been detected in Serratia marcescens Sb. This methylase, M.Smal, modifies the second cytosine residue of the substrate sequence CCCGGG yielding N4-methylcytosine.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom