Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli.
The nature of the energy requirement for irreversible adsorption of phages T1 and phi80 was studied by using various specific energy inhibitors and mutants lacking either the Ca2+, Mg2+-adenosine triphosphatase or the ability to produce cytochromes in the absence of added 5-aminolaevulinic acid. It was found that irreversible adsorption could be energized both through the electron transport chain and from adenosine 5'-triphosphate via the Ca2+, Mg2+-adenosine triphosphatase, indicating the involvement of the energized membrane state. These results and the discovery that phages T1 and phi80 adsorb reversibly to the isolated tonA gene product are discussed in terms of the possible involvement of functions expressed by the tonB gene region in irreversible adsorption and the relationship to iron transport.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000327:Adsorption; D000622:Aminolevulinic Acid / Q000378:metabolism; D001149:Arsenates / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis; D002462:Cell Membrane / Q000378:metabolism / Q000382:microbiology; D003090:Coliphages; D003486:Cyanides / Q000494:pharmacology; D003580:Cytochromes / Q000096:biosynthesis; D004267:DNA Viruses; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D009154:Mutation; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology
D001149:Arsenates; D001426:Bacterial Proteins; D003486:Cyanides; D003580:Cytochromes; D013439:Sulfhydryl Reagents; D014475:Uncoupling Agents; D000622:Aminolevulinic Acid; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases