Molecular analysis of lytic genes of bacteriophage 80 alpha of Staphylococcus aureus.
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.
Bon
J
J
Department of Biological Sciences, Illinois State University, Normal 61790-4120, USA.
Mani
N
N
Jayaswal
R K
RK
D000595:Amino Acid Sequence; D001433:Bacteriolysis; D001483:Base Sequence; D003001:Cloning, Molecular; D005814:Genes, Viral; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics; D017422:Sequence Analysis, DNA; D013204:Staphylococcus Phages / Q000201:enzymology / Q000235:genetics*; D013211:Staphylococcus aureus / Q000821:virology*; D015678:Viral Structural Proteins / Q000235:genetics*
D015678:Viral Structural Proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase