Evidence for an internal component of the bacteriophage T4D tail core: a possible length-determining template.
The length of the T4 tail is precisely regulated in vivo at the time of polymerization of the tail core protein onto the baseplate. Since no mutations which alter tail length have been identified, a study of in vivo-assembled tail cores was begun to determine whether the structural properties of assembled cores would reveal the mechanism of length regulation. An assembly intermediate consisting of a core attached to a baseplate (core-baseplate) was purified from cells infected with a T4 mutant in gene 15. When core-base plates were treated with guanidine hydrochloride, cores were released from baseplates. The released cores had the same mean length as cores attached to baseplates. Electron micrographs of these cores showed partial penetration of negative stain into one end, and, at the opposite end, a modified tip which often appeared as a short fiber projecting from the core. When cores were purified and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, two minor proteins and the major core protein were detected. One minor protein, the product of gene 48 (gp48), was present in at least 72% of the amount found in core-baseplates, relative to the amount of the major core protein. These findings suggest that cores contain a fibrous structure, possibly composed of gp48, which may form a "ruler" that specifies the length of the T4 tail.
D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D009024:Morphogenesis; D011108:Polymers; D013604:T-Phages / Q000032:analysis / Q000378:metabolism / Q000648:ultrastructure*; D013698:Templates, Genetic; D014764:Viral Proteins / Q000502:physiology*
D006146:Guanidines; D011108:Polymers; D014764:Viral Proteins; D019791:Guanidine