The neck of bacteriophage T4 is a ring-like structure formed by a hetero-oligomer of gp13 and gp14.
After packaging of DNA into the head of bacteriophage T4 is completed, a neck is formed at the portal vertex of the head to be ready for the tail attachment. The main components of the neck are gp13 and gp14 (gp: gene product), which consist of 309 and 256 amino acid residues, respectively. In order to elucidate the structure and subunit arrangement in the neck, overexpression systems of gene 13 and gene 14 were constructed and purified to homogeneity. Far-UV circular dichroism (CD) spectra of gp13 and gp14 indicated that gp13 is rich in alpha-helices whereas gp14 is rich in beta-sheets. Sedimentation velocity analysis of gp13 and gp14 revealed that both proteins are present as monomers in solution. The frictional ratios (f/f(0)) of the two proteins indicated that gp14 has a more elongated shape than gp13. Although isolated gp13 and gp14 do not interact with each other when mixed under physiological conditions, they form a hetero-oligomer complex with the stoichiometry of 10:5 after treatment with ammonium sulfate. Electron microscopy of this complex has shown that it forms a ring-like structure of 15 nm in diameter.
Akhter
Tahmina
T
Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4359-B39 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
Zhao
Li
L
Kohda
Atsushi
A
Mio
Kazuhiro
K
Kanamaru
Shuji
S
Arisaka
Fumio
F
D017122:Bacteriophage T4 / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D002942:Circular Dichroism; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism; D019065:Virus Assembly
D046912:Multiprotein Complexes; D014764:Viral Proteins