Molecular analysis of lytic genes of bacteriophage 80 alpha of Staphylococcus aureus

被引:13
作者
Bon, J [1 ]
Mani, N [1 ]
Jayaswal, RK [1 ]
机构
[1] ILLINOIS STATE UNIV, DEPT BIOL SCI, NORMAL, IL 61790 USA
关键词
attachment site; bacteriophage; 80; alpha; holin; peptidoglycan hydrolase; Staphylococcus aureus;
D O I
10.1139/m97-087
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:612 / 616
页数:5
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