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PMID: 128553 Published · ppublish English Journal Article

Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli.

Journal of bacteriology ·Vol. 125 ·No. 2 ·1976-02-00 ·Pages 409-15

Hancock RW, Braun V

Abstract

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.

MeSH Terms
Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Adsorption Aminolevulinic Acid/metabolism Arsenates/pharmacology Bacterial Proteins/biosynthesis Cell Membrane/metabolism,microbiology Coliphages Cyanides/pharmacology Cytochromes/biosynthesis DNA Viruses Electron Transport Escherichia coli/enzymology,metabolism Mutation Sulfhydryl Reagents/pharmacology Uncoupling Agents/pharmacology
Chemicals
Arsenates Bacterial Proteins Cyanides Cytochromes Sulfhydryl Reagents Uncoupling Agents Aminolevulinic Acid Adenosine Triphosphate Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hancock R W
Braun V
References (28)
28 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.125.2.409-415.1976
Published
1976-02-00
Pages
409-15
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC236097
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.125.2.409-415.1976 PMC Full Text View journal details
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