| Development of escherichia coli virus T1. ATP-mediated discrimination of gene expression. | |
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MedLine Citation:
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PMID: 6444298 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The mechanism of host shut-off following virus T1 infection was studied using Escherichia coli wild type and ATPase deficient (unc-) cells. Host protein synthesis measured either as amino acid incorporation into proteins or as enzyme synthesis is immediately inhibited in T1-infected wild type cells. In contrast, host repression in the ATPase-deficient cells is almost unaffected after T1 infection. The continuation of host macromolecule synthesis in the unc- cells is due to constant ATP concentrations after infection, whereas an immediate drop in intracellular ATP levels in T1-infected wild type cells causes repression of host protein synthesis. This result is confirmed when host protein synthesis is determined at decreasing ATP concentrations following the starvation of cells. |
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Authors:
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E F Wagner; M Schweiger |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 255 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1980 Jan |
Date Detail:
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Created Date: 1980-03-24 Completed Date: 1980-03-24 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 540-2 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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metabolism Adenosine Triphosphate / metabolism Bacterial Proteins / biosynthesis Coliphages / metabolism* Escherichia coli / metabolism* Galactokinase / metabolism Glutamine / metabolism Kinetics Virus Replication beta-Galactosidase / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 56-65-5/Adenosine Triphosphate; 56-85-9/Glutamine; EC 2.7.1.6/Galactokinase; EC 3.2.1.23/beta-Galactosidase; EC 3.6.1.-/Adenosine Triphosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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