Morphogenesis of the T4 tail and tail fibers

Characterization of the Helper Proteins for the Assembly of Tail Fibers of Coliphages T4 and l

Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers.

Bacteriophage T4, like all other viruses, is required to be stable while being transmitted from host to host, but also is poised to eject efficiently and rapidly its double-stranded DNA genome to initiate infection. The latter is coordinated by the recognition of receptors on Escherichia coli cells by the long tail fibers and subsequent irreversible attachment by the short tail fibers. These fi...

Isolation and characterization of the bacteriophage T4 tail-associated lysozyme.

Direct evidence has been obtained that the tail-associated lysozyme of bacteriophage T4 (tail-lysozyme) is gp5, which is a protein component of the hub of the baseplate. Tails were treated with 3 M guanidine hydrochloride containing 1% Triton X-100, and the tail-lysozyme was separated from other tail components by preparative isoelectric focusing electrophoresis as a peak with a pI of 8.4. The ...

Processing of the tail lysozyme (gp5) of bacteriophage T4.

The processing site of gp5 has been determined to be between residues Val-390 and His-391, instead of Ser-351 and Ala-352 as previously reported (H. Kanamaru, N. C. Gassner, N. Ye, S. Takeda, and F. Arisaka, J. Bacteriol. 181:2739-2744). Moreover, the maturation of gp5 is abolished by null mutations in other hub genes, indicating that cleavage requires the interactions of several baseplate prot...

Structure of normal and contracted tail sheaths of T4 bacteriophage.

The structural arrangement of protein subunits in extended and contracted tail sheaths of T4 bacteriophage has been studied by optical diffrsctometry of electron micrographs. The analysis of such diffraction patterns shows that the extended sheath consists of annuli of six subunits, these being arranged in a helix of close to seven annuli in two turns. The annuhrs repeat in the helix direction ...