Functional domains of S-type pyocins deduced from chimeric molecules.
Functional domain structures of pyocins AP41, S1, and S2 were assigned by examining the functions of chimeric pyocins and deletion derivatives. Pyocins AP41, S1, and S2 are essentially composed of three domains, the receptor-binding domain, the translocation domain, and the DNase domain, in that order from the N terminus to the C terminus. The alignment of these domains is distinct from that in E2-group colicins with functions similar to those of these pyocins. Pyocins AP41 and S2 have a fourth domain between the receptor-binding and the translocation domains, which is dispensable for their killing functions.
Sano
Y
Y
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
Kobayashi
M
M
Kageyama
M
M
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D005990:Glycerol / Q000378:metabolism; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D010957:Plasmids; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D011709:Pyocins / Q000378:metabolism* / Q000494:pharmacology*; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D015183:Restriction Mapping; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D011709:Pyocins; D011993:Recombinant Fusion Proteins; D005990:Glycerol