rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1992-11-17
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pubmed:abstractText |
Gene 5 protein of bacteriophage T7 is a nonprocessive DNA polymerase. During infection of Escherichia coli, T7 annexes the host protein thioredoxin for use as a processivity factor for T7 DNA polymerase. We describe here a genetic method to investigate the interaction between T7 gene 5 protein and E. coli thioredoxin. The strategy is to use thioredoxin mutants that are unable to support the growth of wild-type T7 phage to select for T7 revertant phage that suppress the defect in thioredoxin. A thioredoxin mutation that replaces glycine at position 74 with aspartic acid fails to support the growth of wild-type T7. This mutation is suppressed by six different mutations within T7 gene 5, each of which results in a single amino acid substitution within gene 5 protein. Three of the suppressor mutations are located within the putative polymerization domain of gene 5 protein, and three are located within the putative 3'-to-5' exonucleolytic domain. Each suppressor mutation alone is necessary and sufficient to confer the revertant phenotype.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1095578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1569092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1657977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1671045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1682322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1846298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1967833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-1988449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2020551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2050671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2055476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2173776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2181145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2193685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2703498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2790959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2832946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2882424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2902631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-2985538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-3029683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-3100913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-3316214,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-6971292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1409697-768986
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
89
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pubmed:geneSymbol |
gene 5,
trxA
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9774-8
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1409697-DNA Replication,
pubmed-meshheading:1409697-DNA-Directed DNA Polymerase,
pubmed-meshheading:1409697-Escherichia coli,
pubmed-meshheading:1409697-Genes, Suppressor,
pubmed-meshheading:1409697-Genetic Complementation Test,
pubmed-meshheading:1409697-Macromolecular Substances,
pubmed-meshheading:1409697-Mutagenesis, Site-Directed,
pubmed-meshheading:1409697-Mutation,
pubmed-meshheading:1409697-Protein Structure, Tertiary,
pubmed-meshheading:1409697-Structure-Activity Relationship,
pubmed-meshheading:1409697-T-Phages,
pubmed-meshheading:1409697-Thioredoxins,
pubmed-meshheading:1409697-Viral Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Genetic analysis of the interaction between bacteriophage T7 DNA polymerase and Escherichia coli thioredoxin.
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pubmed:affiliation |
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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