The host specificity system in Escherichia coli SK

Abstract

E. coli SK has its own enzyme system providing DNA host specificity which differs from the known types of specificity in E. coli K12 and E. coli B. Modification and restriction are observed when the PBVI or PBV3 phages are transferred from E. coli SK to E. coli B or K12 (and back). A methylase has been isolated from E. coli SK cells and partly purified. This methylase catalyzes in vitro transfer of the labelled methyl groups from S-adenosylmethionine (SAM) to DNA of both phage and tissue origin which gives rise to 5'-methylcytosine (5'MC) and 6'-methylaminopurine (6'MAP). The methylase preparations isolated from the cells at the stationary growth have proved to be 1.5-1.7 times as active as the enzyme from the cells at the logarithmic growth stage. The extract of E. coli SK cells infected with the phage SD cannot methylate DNA in vitro. This fact is due to de novo synthesis of the enzyme which disintegrates SAM down to 5'-methyltioadenosine (5'MTA) and homoserine (HS). This enzyme is not found in the cells infected with the SD phage in the presence of chloroamphenicole. The activity of the enzyme which disintegrates SAM is the highest between the 4th and the 5th minutes of infection. Thus it may be assumed that this enzyme, most probably, is an early virus specific protein and prevents in vivo methylation of the phage DNA.