Studies related to the head‐maturation pathway of bacteriophages T4 and T2: II. Nuclear disruption, protein synthesis and particle formation with the mutant 43−·30−·46−

Wunderli, Heidi; Couture, E.; Vince, Daphne; Kellenberger, E.

doi:10.1002/jss.400070203

Cited by 9 publications

(2 citation statements)

References 38 publications

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“…A total of 930 copies of the gp23 and 55 copies of gp24 are needed for the assembly of the prohead [24,28–29]. The volume of the prohead is approximately 15–20% smaller than that of the mature head [55–57]. The gp21 is then self-cleaved and activated to become a protease (T4PPase) in the prohead [58–62].…”

Section: Head Structurementioning

confidence: 99%

Structure and Function of Bacteriophage T4

2014

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Bacteriophage T4 is the most well-studied member of Myoviridae, the most complex family of tailed phages. T4 assembly is divided into three independent pathways: the head, the tail and the long tail fibers. The prolate head encapsidates a 172 kbp concatemeric dsDNA genome. The 925 Å-long tail is surrounded by the contractile sheath and ends with a hexagonal baseplate. Six long tail fibers are attached to the baseplate’s periphery and are the host cell’s recognition sensors. The sheath and the baseplate undergo large conformational changes during infection. X-ray crystallography and cryo-electron microscopy have provided structural information on protein–protein and protein–nucleic acid interactions that regulate conformational changes during assembly and infection of Escherichia coli cells.

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Section: Head Structurementioning

confidence: 99%

Structure and Function of Bacteriophage T4

2014

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“…4a. Both types of particles have also been observed in lysates of 17--infected cells (46) and were identified as empty large and empty small particles, respectively; both were shown to be made with gp23* (4; Wunderli, thesis).…”

Section: Downloaded Frommentioning

confidence: 99%

Head maturation pathway of bacteriophages T4 and T2. V. Maturable epsilon-particle accumulating an acridine-treated bacteriophage T4-infected cells

Schaerli¹,

Kellenberger²

1980

J Virol

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A maturable head-related particle of bacteriophage T4 has been identified and characterized. This e-particle has the same size as the prehead, but its shell is made of the cleaved product of gene 23 (gp23*). It contains internal matter, most likely the processed core proteins, which is lost or modified by experimental manipulation. It accumulates, together with partially filled ("grizzled") heads, in T4-infected cells that are treated with 9-aminoacridine. On sections of "wellpreserved" cells the E-particles are not identifiable with certainty; a more or less empty breakdown product of them becomes visible when cytoplasmic leakage is induced. The number of particles per cell is then in agreement with the biochemically determined amount of gp23* and with the number of particles counted in lysates. Morphologically and biochemically, the isolated e-particles closely resemble the empty small particles of 17--infected cells described in previous papers of this series. Both are composed of gp23* and are still unexpanded, so that they are not yet able to bind the minor head proteins soc and hoc. We discuss the possibility of the e-particle being an intermediate on the normal T4 wild-type head maturation pathway.The DNA-containing head of bacteriophage T4 appears to mature out of a proteinous prehead (1,2,23,38). Maturation involves the following events: (i) processing of the shell proteins (gp23, gp24) and of the core proteins (gp22 and internal proteins); (ii) expansion by 15% in linear dimensions; and (iii) packaging of DNA. It is not

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Studies related to the head‐maturation pathway of bacteriophages T4 and T2: I. Morphology and kinetics of intracellular particles produced by mutants in the maturation genes

Wunderli

Kellenberger

1977

J Supramol Struct

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Mutants in the genes governing the maturation of the head of bacteriophage T4 and in gene 24 were studied by electron microscopy of thin sections. We define morphologically: black particles, comprising mature, stable heads and immature, fragile heads, which break down upon lysis; grizzled particles, which apparently are partially filled or partially emptied; empty large particles without DNA or core which are all the same size as normal heads; empty small particles without DNA and without core which are of the size of the tau particle, which is the prehead of phage T4. The study of single and double mutants of the maturation genes demonstrates that the phenotypes are only different by the proportions of the different particles made except for 17- where only empty small and empty large particles accumulate. The mutants in gene 24 are epistatic on all other mutants. Mutants in gene 17 are epistatic on the remaining ones. The results are consistent with the hypothesis that the products of several of the maturation genes act on DNA to render it competent for packaging while the others act directly on the particle. By this uncoupling, bypasses and abortive pathways can result.

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Studies related to the head‐maturation pathway of bacteriophages T4 and T2: II. Nuclear disruption, protein synthesis and particle formation with the mutant 43⁻·30⁻·46⁻

Cited by 9 publications

References 38 publications

Structure and Function of Bacteriophage T4

Structure and Function of Bacteriophage T4

Head maturation pathway of bacteriophages T4 and T2. V. Maturable epsilon-particle accumulating an acridine-treated bacteriophage T4-infected cells

Studies related to the head‐maturation pathway of bacteriophages T4 and T2: I. Morphology and kinetics of intracellular particles produced by mutants in the maturation genes

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