Source:http://linkedlifedata.com/resource/pubmed/id/15251197
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-7-14
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pubmed:abstractText |
A chloramphenicol acetyltransferase (catB7) gene containing two point mutations, 181A/G and 314A/G, has been recently reported to be a determinant for high-level chloramphenicol resistance phenotype in a Pseudomonas aeruginosa strain PAhcr1. The mutant CATB7 was further characterized in vitro and in vivo to elucidate the molecular basis of high-level resistance. CAT assay demonstrated that the mutant and wild-type recombinant CATB7 had similar specific activities. Dot blotting revealed that the accumulated amounts of CATB7 in P. aeruginosa strains PAO1 and PAhcr1 were proportionate to the respective anti-chloramphenicol level. Site-directed mutagenesis showed that G61S and Y105C contributed synergistically to the PAhcr1 resistance phenotype. It could be proposed that the mutant CATB7 was more structurally stable than catalytically efficient as a chloramphenicol resistance determinant in PAhcr1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0378-1097
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
236
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
197-204
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15251197-Acetyl Coenzyme A,
pubmed-meshheading:15251197-Amino Acid Substitution,
pubmed-meshheading:15251197-Bacterial Proteins,
pubmed-meshheading:15251197-Chloramphenicol,
pubmed-meshheading:15251197-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:15251197-Chloramphenicol Resistance,
pubmed-meshheading:15251197-Cloning, Molecular,
pubmed-meshheading:15251197-Enzyme Stability,
pubmed-meshheading:15251197-Genes, Bacterial,
pubmed-meshheading:15251197-Microbial Sensitivity Tests,
pubmed-meshheading:15251197-Mutagenesis, Site-Directed,
pubmed-meshheading:15251197-Mutation,
pubmed-meshheading:15251197-Pseudomonas aeruginosa,
pubmed-meshheading:15251197-Recombinant Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Mutations in the chloramphenicol acetyltransferase (S61G, Y105C) increase accumulated amounts and resistance in Pseudomonas aeruginosa.
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pubmed:affiliation |
School of Life Science & Technology, Shanghai Jiaotong University, No. 800 Dong-Chuan Road, Shanghai 200240, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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