Cloning and characterization of M.LmoA118I, a novel DNA:m4C methyltransferase from the Listeria monocytogenes phage A118, a close homolog of M.NgoMXV.
A homolog of M.NgoMXV DNA:m4C methyltransferase has been identified among the open reading frames deduced from the genomic sequence of Listeria monocytogenes phage A118 [Loessner et al., 2000]. The gene coding for this putative protein has been cloned in Escherichia coli and its enzymatic activity in vivo in this host have been analyzed. Remarkably, despite M.NgoMXV and M.LmoA118I exhibit high sequence similarity (58% identical and 19% conservatively substituted residues), their target preferences differ: both proteins exhibit "relaxed" sequence specificity, but while M.LmoA118I more efficiently methylates GGCC sites, it seems to target only a subset of CCWGG sites methylated by M.NgoMXV.
Bujnicki
J M
JM
Bioinformatics Laboratory, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Radlinska
M
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics; D004587:Electrophoresis, Agar Gel; D004926:Escherichia coli / Q000235:genetics; D008089:Listeria monocytogenes / Q000235:genetics / Q000821:virology*; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D004279:DNA, Viral; D008780:Methyltransferases