Irreversible binding of bacteriophage T5 to its FhuA receptor protein is associated with covalent cross-linking of 3 copies of tail protein pb4.
Irreversible binding of bacteriophage T5 to its FhuA receptor protein is characterized by a high activation energy, typical for reactions where covalent bonds are formed [Zarnitz, M.L. and Weidel, W. (1963) Z. Naturforsch. 18b, 276-280]. Upon binding of radiolabeled T5 phages to FhuA formation of a new protein of 250 kDa was observed. Using electrophoretical and Western blotting techniques this protein was shown to be formed by cross-linking of 3 copies of tail protein pb4, rather than by cross-linking of FhuA and the receptor-binding protein.
Feucht
A
A
Universität Konstanz, Fakultät für Biologie, Konstanz, FRG.
Heinzelmann
G
G
Heller
K J
KJ
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008970:Molecular Weight; D011485:Protein Binding; D011991:Receptors, Virus; D013604:T-Phages / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*; D017376:Viral Tail Proteins
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C050900:FhuA protein, E coli; D011991:Receptors, Virus; D014764:Viral Proteins; D017376:Viral Tail Proteins