Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites.
We constructed a set of deletion mutants in the attachment protein of phage fd. These mutants lack sequences coding for sections in the amino-terminal half. All the mutants that comprise a leader sequence are incorporated into phage particles. Our data strongly suggest a bipartite organization of the amino-terminal domain with (1) a region for receptor recognition and (2) a region that is necessary for penetration of the DNA into the host cell. These regions were mapped. Some evidence suggesting different roles for gene 3 protein in penetration of the outer and inner membrane are discussed. We demonstrate that the phenotypes caused by gene 3 protein in host cells can be subdivided into two groups with different sequence requirements: (1) phenotypes related to outer membrane disturbance; and (2) phenotypes related to the tolQRA transport system.
Stengele
I
I
Fakultät für Biologie, Universität Konstanz, West Germany.
Bross
P
P
Garcés
X
X
Giray
J
J
Rasched
I
I
D000595:Amino Acid Sequence; D001287:Attachment Sites, Microbiological / Q000235:genetics*; D001483:Base Sequence; D002213:Capsid / Q000235:genetics*; D002872:Chromosome Deletion; D003090:Coliphages / Q000502:physiology*; D008242:Lysogeny / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D014161:Transduction, Genetic