Mass distribution of a probable tail-length-determining protein in bacteriophage T4.
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 کاملProcessing 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...
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 کاملThe tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria.
The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central non-contractile tail tube. The contraction of the shea...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1985
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.82.16.5550