Intracellular events in canavanine-treated, T4-infected Escherichia coli

Couse, N.L.; Haworth, Philip; Moody, W. G.; Cummings, Donald J.

doi:10.1016/0042-6822(72)90430-8

Cited by 13 publications

(11 citation statements)

References 6 publications

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“…Canavanine can be incorporated into T4 proteins (7,9) and the incorporation of canavanine into an enzyme could conceivably lead to its inactivation. The gene 21-dependent proteolytic activity is clearly inhibited in extracts from canavanine-treated infected cells and the activity is detectable in extracts from cells treated with arginine after the canavanine treatment.…”

Section: Resultsmentioning

confidence: 99%

“…L-Canavanine has been shown to interfere with the normal growth and maturation of T-even bacteriophages (3,6,7,10). The exposure of an infected cell to L-canavanine results in the arrest of a critical function which is required to control the normal head length of the virus (4).…”

mentioning

confidence: 99%

“…Canavanine also markedly inhibits the synthesis of viral DNA (3, 7) and it prevents the viral-induced stimulation of polyamine synthesis (5). However, canavanine does not affect net viral RNA or protein synthesis (7). The normal cleavages of viral proteins are inhibited, indicating that canavanine prevents the normal morphogenesis of the head (4,6,9).…”

mentioning

confidence: 99%

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Structural aberrations in T-even bacteriophage. VII. In vitro analysis of the canavanine-mediated inhibition of proteolytic cleavage

Bolin¹,

Cummings²

1975

J Virol

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Canavanine arrests a critical function in head morphogenesis and the potential for forming giant T-even phage particles termed lollipops is induced. Formation of the particles requires the addition of arginine and the restoration of normal functions. We now report on an investigation into the effects of canavanine on both the T4-induced proteolytic activity and on the substrate proteins. Using an in vitro cleavage assay we have shown that the gene 21-dependent proteolytic activity from canavanine-treated extracts is markedly inhibited, whereas the substrate proteins retain a high susceptibility for cleavage. The proteolytic activity in extracts treated with canavanine followed by arginine is readily detectable, and proteins previously synthesized in the presence of canavanine can be cleaved. Protein synthesis is apparently required for the appearance of the proteolytic activity after the canavanine-arginine treatment. Mixing experiments suggest the requirement for a component of the gene 21-dependent proteolytic activity that is not coded for by gene 21.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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Structural aberrations in T-even bacteriophage. VII. In vitro analysis of the canavanine-mediated inhibition of proteolytic cleavage

Bolin¹,

Cummings²

1975

J Virol

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“…Total RNA synthesis was unaffected, whereas DNA synthesis was inhibited about 70%o as compared with the normal phage culture (26). More importantly, total protein synthesis, in spite of a 200-fold reduction in bacteriophage yield, was unaffected (25,26,29). We Autoradiogram of an SDS-10% polyacrylamide slab gel showing the effect of an inhibition of cleavage on the appearance ofthe alt protein.…”

Section: Ia Ulljdmentioning

confidence: 99%

“…(Kindly provided by the Information Theory Group, Basel.) 26. Surface lattice structures of four different types of giant phage capsids, obtained by computer filtration of electron micrographs.…”

Section: Properties Of Giantsmentioning

confidence: 99%