منابع مشابه
Morphological localization of the bacteriophage tail enzyme.
In an earlier report dealing with the chemistry of viral invasion, Barrington and Kozloff (1,2) showed that incubat,ion of various T series bacteriophages with N16-labeled Escherichiu coli B cell walls caused the release of as much as 15 per cent of the total nitrogen from the host cell walls. The characteristics of this interaction appeared to be similar to those of an enzymatic reaction, and ...
متن کاملStructure of bacteriophage SPP1 tail reveals trigger for DNA ejection.
The majority of known bacteriophages have long noncontractile tails (Siphoviridae) that serve as a pipeline for genome delivery into the host cytoplasm. The tail extremity distal from the phage head is an adsorption device that recognises the bacterial receptor at the host cell surface. This interaction generates a signal transmitted to the head that leads to DNA release. We have determined str...
متن کاملIsolation 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 ...
متن کاملConserved translational frameshift in dsDNA bacteriophage tail assembly genes.
A programmed translational frameshift similar to frameshifts in retroviral gag-pol genes and bacterial insertion elements was found to be strongly conserved in tail assembly genes of dsDNA phages and to be independent of sequence similarities. In bacteriophage lambda, this frameshift controls production of two proteins with overlapping sequences, gpG and gpGT, that are required for tail assembl...
متن کاملStructure and functions of the bacteriophage P22 tail protein.
The product of gene 9 (gp9) of Salmonella typhimurium bacteriophage P22 is a multifunctional structural protein. This protein is both a specific glycosidase which imparts the adsorption characteristics of the phage for its host and a protein which participates in a specific assembly reaction during phage morphogenesis. We have begun a detailed biochemical and genetic analysis of this gene produ...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1970
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.5.6.726-739.1970