Bon J, Mani N, Jayaswal R K
Department of Biological Sciences, Illinois State University, Normal 61790-4120, USA.
Can J Microbiol. 1997 Jul;43(7):612-6. doi: 10.1139/m97-087.
Nucleotide sequencing of a 3779-bp fragment of the Staphylococcus aureus bacteriophage 80 alpha revealed two open reading frames: ORF1, designated as lytA, which encodes a polypeptide of 481 amino acids with an apparent M(r) of 53.81 kDa; and ORF2, designated as holin, which encodes for a hydrophobic polypeptide of 145 amino acids with an apparent M(r) of 15.58 kDa and exhibits two putative transmembrane helices. Both genes showed 100% sequence homology to that of the peptidoglycan hydrolase and holin genes of the S. aureus phage phi 11 reported earlier. In addition, the downstream sequences of the lytA gene were homologous to the phage attachment site (attP) of the phage phi 11. Based on our data we propose that the lytic system of the phage 80 alpha evolved from that of phage phi 11.
对金黄色葡萄球菌噬菌体80α的一个3779碱基对片段进行核苷酸测序,发现了两个开放阅读框:ORF1,命名为lytA,编码一个481个氨基酸的多肽,表观分子量为53.81 kDa;以及ORF2,命名为holin,编码一个145个氨基酸的疏水多肽,表观分子量为15.58 kDa,并呈现出两个推定的跨膜螺旋。这两个基因与先前报道的金黄色葡萄球菌噬菌体phi 11的肽聚糖水解酶和holin基因的序列同源性均为100%。此外,lytA基因的下游序列与噬菌体phi 11的噬菌体附着位点(attP)同源。基于我们的数据,我们提出噬菌体80α的裂解系统是从噬菌体phi 11进化而来的。