Sequence of the Salmonella typhimurium StyLT1 restriction-modification genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence of helicase domains.
The StyLT1 restriction-modification (R-M) system of Salmonella typhimurium has recently been suggested to belong to the type-III R-M systems [De Backer and Colson, Gene 97 (1991) 103-107]. The nucleotide sequences of StyLT1 mod and res have been determined. Two closely adjacent open reading frames were found 12 bp apart with coding capacities of 651 (Mod) and 982 (Res) amino acids (aa), respectively. The genes, lying in the same direction of transcription in the mod-res order, are transcribed as distinct units. The deduced aa sequences reveal homologies with known type-III enzymes from the Escherichia coli P1 prophage, E. coli P15 plasmid and Bacillus cereus chromosome. In addition, the StyLT1 restriction endonuclease (ENase), like other type-I and type-III ENases, contains sequence motifs characteristic of superfamily-II helicases, which may be involved in DNA unwinding at the cleavage site.
Dartois
V
V
Unité de Génétique, Université Catholique de Louvain, Belgium.
De Backer
O
O
Colson
C
C
D000595:Amino Acid Sequence; D001483:Base Sequence; D017124:Conserved Sequence; D004265:DNA Helicases / Q000235:genetics* / Q000378:metabolism; D004269:DNA, Bacterial; D015263:Deoxyribonucleases, Type III Site-Specific / Q000235:genetics* / Q000378:metabolism; D008780:Methyltransferases; D008969:Molecular Sequence Data; D012486:Salmonella typhimurium / Q000201:enzymology / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000235:genetics* / Q000378:metabolism
D004269:DNA, Bacterial; C067137:DNA modification methylase StyLTI; D008780:Methyltransferases; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); C030432:endodeoxyribonuclease EcoP1; C023451:endodeoxyribonuclease EcoP15I; C067136:endodeoxyribonuclease StyLTI; D015263:Deoxyribonucleases, Type III Site-Specific; D004265:DNA Helicases