Bacteriophage T4 Self-Assembly: Localization of gp3 and Its Role in Determining Tail Length
نویسندگان
چکیده
منابع مشابه
Mass distribution of a probable tail-length-determining protein in bacteriophage T4.
Analysis of dark-field scanning transmission electron micrographs of unstained freeze-dried specimens established that the interior of the intact bacteriophage T4 tail tube contains extra density that is missing in tubes artificially emptied by treatment with 3 M guanidine hydrochloride. The mass of the tail tube is 3.1 X 10(6) daltons, and the central channel is 3.2 nm in diameter. Quantitativ...
متن کاملRole of bacteriophage T4 baseplate in regulating assembly and infection.
Bacteriophage T4 consists of a head for protecting its genome and a sheathed tail for inserting its genome into a host. The tail terminates with a multiprotein baseplate that changes its conformation from a "high-energy" dome-shaped to a "low-energy" star-shaped structure during infection. Although these two structures represent different minima in the total energy landscape of the baseplate as...
متن کاملStructure 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 ...
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 کاملThree-Dimensional Rearrangement of Proteins in the Tail of Bacteriophage T4 on Infection of Its Host
The contractile tail of bacteriophage T4 undergoes major structural transitions when the virus attaches to the host cell surface. The baseplate at the distal end of the tail changes from a hexagonal to a star shape. This causes the sheath around the tail tube to contract and the tail tube to protrude from the baseplate and pierce the outer cell membrane and the cell wall before reaching the inn...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2000
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.182.3.680-688.2000