SEQUENCE OF THE SALMONELLA-TYPHIMURIUM STYLT1 RESTRICTION-MODIFICATION GENES - HOMOLOGIES WITH ECOP1 AND ECOP15 TYPE-III R-M SYSTEMS AND PRESENCE OF HELICASE DOMAINS
V. Dartois et al., SEQUENCE OF THE SALMONELLA-TYPHIMURIUM STYLT1 RESTRICTION-MODIFICATION GENES - HOMOLOGIES WITH ECOP1 AND ECOP15 TYPE-III R-M SYSTEMS AND PRESENCE OF HELICASE DOMAINS, Gene, 127(1), 1993, pp. 105-110
The StyLT1 restriction-modification (R-M) system of Salmonella typhimu
rium has recently been suggested to belong to the type-III R-M systems
[De Backer and Colson, Gene 97 (1991) 103-107]. The nucleotide sequen
ces of StyLT1 mod and res have been determined. Two closely adjacent o
pen reading frames were found 12 bp apart with coding capacities of 65
1 (Mod) and 982 (Res) amino acids (aa), respectively. The genes, lying
in the same direction of transcription in the mod-res order, are tran
scribed 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 StyL
T1 restriction endonuclease (ENase), like other type-I and type-III EN
ases, contains sequence motifs characteristic of superfamily-II helica
ses, which may be involved in DNA unwinding at the cleavage site.