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Protection from proteolysis using a T4::T7-RNAP phage expression-packaging-processing system

Autor: Y R, Hong, J M, Mullaney, L W, Black

Publikováno v: Gene. 162(1)

DNA coding for bacteriophage T7 RNA polymerase (T7-RNAP) was inserted into a positive selection-vector form of the T4 genome, placing it under the control of bacteriophage T4 ipIII promoters. The recombinant T4::T7-RNAP fusion phage retained infectiv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::39911b797a2a4e5978becaa458d1b82a
https://pubmed.ncbi.nlm.nih.gov/7557416

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Bacteriophage T4 gene 17 amplification mutants: evidence for initiation by the T4 terminase subunit gp16

Autor: C H, Wu, H, Lin, L W, Black

Publikováno v: Journal of molecular biology. 247(4)

Bacteriophage T4 genes 16 and 19 containing the 24 bp homology regions that recombine to form Hp17 mutants were cloned into plasmids. When the two homology sequences were cloned either together into one or separately into two compatible plasmids, a p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d65c405867249ccc7e55c0ff44a27643
https://pubmed.ncbi.nlm.nih.gov/7723009

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Mutational analysis of the sequence-specific recombination box for amplification of gene 17 of bacteriophage T4

Autor: C H, Wu, L W, Black

Publikováno v: Journal of molecular biology. 247(4)

Bacteriophage T4 gene 17 amplification mutants Hp17 that carry two to six tandem repeats of the genes 17-18 region were isolated by growth of gene 17 amber mutants on ochre suppressor strains of Escherichia coli. These mutants arise from an initial s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::96c89953f1c46b2764fec32b19dadf56
https://pubmed.ncbi.nlm.nih.gov/7723018

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Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, co-operativity, and super-stabilization by soc binding

Autor: A C, Steven, H L, Greenstone, F P, Booy, L W, Black, P D, Ross

Publikováno v: Journal of molecular biology. 228(3)

We have used differential scanning calorimetry in conjunction with cryo-electron microscopy to investigate the conformational transitions undergone by the maturing capsid of phage T4. Its precursor shell is composed primarily of gp23 (521 residues):

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6692a44fa3b9c7727eb2d96d529c07ce
https://pubmed.ncbi.nlm.nih.gov/1469720

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Isolation and characterization of a portal protein-DNA complex from dsDNA bacteriophage

Autor: A, Zachary, L W, Black

Publikováno v: Intervirology. 33(1)

A portal protein-DNA complex was isolated from bacteriophage disrupted in 70% acetic acid. This treatment dissociated most of the phage structural proteins, while the portal protein ring remained attached to the highly condensed naked DNA. In the abs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2088f32b2cf07de348361c4047c6cc4f
https://pubmed.ncbi.nlm.nih.gov/1740384

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Purification and properties of the bacteriophage T4 gene 31 protein required for prehead assembly

Autor: L W Black, C J Castillo

Publikováno v: Journal of Biological Chemistry. 253:2132-2139

A low molecular weight (approximately 16,000), early protein is characterized as the product of the essential T4 head assembly gene 31. This gene is known to be required to allow formation of any ordered head structure from the major T4 capsid protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8dbed398deb5654276661596e92c2424
https://doi.org/10.1016/s0021-9258(17)38050-x

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UV irradiation impairs in vivo encapsidation of bacteriophage T4 DNA

Autor: L W Black, A Zachary

Publikováno v: Journal of Virology. 50:293-300

T4 DNA structural requirements for encapsidation in vivo were investigated, using thin-section electron microscopy to quantitate the kinetics and yields of head intermediates after synchronous DNA packaging into accumulated processed proheads. UV irr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78c0478742c678762000887bab9e46d1
https://doi.org/10.1128/jvi.50.2.293-300.1984

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Head morphologies in bacteriophage T4 head and internal protein mutant infections

Autor: L W Black, D T Brown

Publikováno v: Journal of Virology. 17:894-905

Escherichia coli infected with phage T4 mutants defective in synthesis of the three major internal proteins found in the phage head, IPI-, IPII-, IPIII-, or IP degrees (lacking all three) were examined in the electron microscope for head formation. I

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5108f66e5987a53be5a9842466d3c5a2
https://doi.org/10.1128/jvi.17.3.894-905.1976

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A bacteriophage T4 DNA packaging related DNA-dependent ATPase-endonuclease

Autor: V Manne, V B Rao, L W Black

Publikováno v: Journal of Biological Chemistry. 257:13223-13232

A new bacteriophage T4-induced DNA-dependent ATPase-endonuclease was purified to essential homogeneity from an extract of late infected Escherichia coli. Both DNA-dependent ATPase and endonuclease activities co-chromatograph, co-sediment, and have be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7c88b8dd5d128e3322096b629762ce0b
https://doi.org/10.1016/s0021-9258(18)33434-3

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