Functional domains of colicin A.
A large number of mutations which introduce deletions in colicin A have been constructed. The partially deleted colicin A proteins were purified and their activity in vivo (on sensitive cells) and in vitro (in planar lipid bilayers) was assayed. The receptor-binding properties of each protein were also analysed. From these results, we suggest that the NH2-terminal region of colicin A (residues 1 to 172) is involved in the translocation step through the outer membrane. The central region of colicin A (residues 173 to 336) contains the receptor-binding domain. The COOH-terminal domain (residues 389 to 592) carries the pore-forming activity.
Baty
D
D
Centre de Biochimie et de Biologie Moléculaire du C.N.R.S., Marseille, France.
Frenette
M
M
Lloubès
R
R
Geli
V
V
Howard
S P
SP
Pattus
F
F
Lazdunski
C
C
D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D002872:Chromosome Deletion; D003087:Colicins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D009154:Mutation; D015183:Restriction Mapping
D003087:Colicins