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Identification of a subdomain within DNA‐(cytosine‐C5)‐methyltransferases responsible for the recognition of the 5′ part of their DNA target.
Author(s) -
Lange C.,
Wild C.,
Trautner T. A.
Publication year - 1996
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.1460-2075.1996.tb00486.x
Subject(s) - biology , methyltransferase , cytosine , dna , genetics , identification (biology) , 5 methylcytosine , computational biology , dna methylation , gene , methylation , gene expression , botany
In previous work on DNA‐(cytosine‐C5)‐methyltransferases (C5‐MTases), domains had been identified which are responsible for the sequence specificity of the different enzymes (target‐recognizing domains, TRDs). Here we have analyzed the DNA methylation patterns of two C5‐MTases containing reciprocal chimeric TRDs, consisting of the N‐ and C‐terminal parts derived from two different parental TRDs specifying the recognition of 5′‐CC(A/T)GG‐3′ and 5′‐GCNGC‐3′. Sequences recognized by these engineered MTases were non‐symmetrical and degenerate, but contained at their 5′ part a consensus sequence which was very similar to the 5′ part of the target recognized by the parental TRD which contributed the N‐terminal moiety of the chimeric TRD. The results are discussed in connection with the present understanding of the mechanism of DNA target recognition by C5‐MTases. They demonstrate the possibility of designing C5‐MTases with novel DNA methylation specificities.