Publications

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amber suppressor mutations in pseudomonas acidovorans.almost 50% of the clones of pseudomonas acidovorans(plm2) selected for resistance to tetracycline supported the growth of an amber mutant of bacteriophage prd1.1979370094
characterization of a dna binding protein of bacteriophage prd1 involved in dna replication.escherichia coli phage prd1 protein p12, involved in prd1 dna replication in vivo, has been highly purified from e. coli cells harbouring a gene xii-containing plasmid. protein p12 binds to single-stranded dna as shown by gel retardation assays and nuclease protection experiments. binding of protein p12 to single-stranded dna increases about 14% the contour length of the dna as revealed by electron microscopy. binding to single-stranded dna seems to be cooperative, and it is not sequence specifi ...19902251117
the genome of lipid-containing bacteriophage prd1, which infects gram-negative bacteria, contains long, inverted terminal repeats.the bacteriophage prd1 is a lipid-bearing phage that infects a wide variety of gram-negative bacteria, including escherichia coli and salmonella typhimurium when they contain the appropriate plasmid. it contains a linear duplex dna molecule that is covalently bound by its 5' ends to a terminal protein. we report here that the prd1 genome contains a 111-base-pair terminal inverted repeat which does not bear homology to that of any known linear duplex dnas with terminal proteins. we further report ...19873543400
structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses.archaea and their viruses are poorly understood when compared with the eukarya and bacteria domains of life. we report here the crystal structure of the major capsid protein (mcp) of the sulfolobus turreted icosahedral virus, an archaeal virus isolated from an acidic hot spring (ph 2-4, 72-92 degrees c) in yellowstone national park. the structure is nearly identical to the mcp structures of the eukaryotic paramecium bursaria chlorella virus, and the bacteriophage prd1, and shows a common fold wi ...200516357204
purification and characterization of the assembly factor p17 of the lipid-containing bacteriophage prd1.assembly factors, proteins assisting the formation of viral structures, have been found in many viral systems. the gene encoding the assembly factor p17 of bacteriophage prd1 has been cloned and expressed in escherichia coli. p17 acts late in phage assembly, after capsid protein folding and multimerization, and sorting of membrane proteins has occurred. p17 has been purified to near homogeneity. it is a tetrameric protein displaying a rather high heat stability. the protein is largely in an alph ...199910095794
identification and functional analysis of the rz/rz1-like accessory lysis genes in the membrane-containing bacteriophage prd1.bacteriophage prd1 is a tailless membrane-containing double-stranded (ds) dna virus infecting a variety of gram-negative bacteria. in order to affect cell lysis, like most dsdna phages, prd1 uses the holin-endolysin system. in this study, we identified two accessory lysis genes, xxxvi and xxxvii, coding for proteins p36 and p37, respectively. using genetic complementation assays, we show that protein pair p36/p37 is a functional and interchangeable analogue of the rz/rz1 of bacteriophage lambda. ...200818366440
identification and mutational analysis of bacteriophage prd1 holin protein p35.holin proteins are phage-induced integral membrane proteins which regulate the access of lytic enzymes to host cell peptidoglycan at the time of release of progeny viruses by host cell lysis. we describe the identification of the membrane-containing phage prd1 holin gene (gene xxxv). the prd1 holin protein (p35, 12.8 kda) acts similarly to its functional counterpart from phage lambda (gene s), and the defect in prd1 gene xxxv can be corrected by the presence of gene s of lambda. several nonsense ...200312813073
isolation of a phospholipid-free protein shell of bacteriophage prd1, an escherichia coli virus with an internal membrane.prd1 is a double-stranded dna virus infecting escherichia coli and salmonella typhimurium. it has an icosahedral outer protein capsid which encloses the viral membrane, inside of which resides the phage genome. in this investigation we demonstrate the detergent resistance of the intact virus particles. the membrane of empty dna-free particles, however, is very sensitive to detergent action. we assume that their sensitivity is due to the access of detergents through a portal structure to the viru ...19938503174
establishment of a physical and genetic map for bacteriophage prd1.dna was isolated from the lipid-containing bacteriophage prd1 and subjected to restriction endonuclease analysis. the total genome size is 14.7 kb. prd1 dna was resistant to cutting by fifteen restriction endonucleases with six base specificity. haeii made thirty-seven cuts in the dna, mboi made one cut, and mnli made six cuts. dna that was not treated with protease yielded two fewer fragments when treated with haeii. evidence is presented to indicate that the prd1 dna has protein at the ends of ...19836308389
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