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The EcoA restriction and modification system of Escherichia coli 15T‐: enzyme structure and DNA recognition sequence.
Author(s) -
Suri B.,
Shepherd J.C.,
Bickle T.A.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01850.x
Subject(s) - biology , escherichia coli , recognition sequence , restriction enzyme , dna , sequence (biology) , escherichia coli proteins , genetics , enzyme , restriction map , base sequence , microbiology and biotechnology , computational biology , gene , biochemistry
The EcoA restriction enzyme from Escherichia coli 15T‐ has been isolated. It proves to be an unusual enzyme, clearly related functionally to the classical type I restriction enzymes. The basic enzyme is a two subunit modification methylase. Another protein species can be purified which by itself has no enzymatic activities but which converts the modification methylase to an ATP and S‐adenosylmethionine‐dependent restriction endonuclease. The DNA recognition sequence of EcoA has an overall structure that is very similar to previously determined type I sequences. It is: 5′‐GAGGTCA‐3′ 3′‐CTCCAGT‐5′ where N can be any nucleotide. Modification methylates the adenosyl residue in the specific trinucleotide and the adenosyl residue in the lower strand of the specific tetranucleotide.