Isolation and characterization of OmpC porin mutants with altered pore properties
The LamB protien is normally required for the uptake of maltodextrins. Starting with a LamB/sup -/ OmpF/sup -/ strain, we have isolated mutants that will grow on maltodextrins. The mutation conferring the Dex/sup +/ phenotype in the majority of these mutants has been mapped to the ompC locus. These mutants, unlike LamB/sup -/ OmpF/sup -/ strains, grew on maltotriose and maltotetraose, but not on maltopentaose, and showed a significantly higher rate of (/sup 14/C) maltose uptake than the parent strain did. In addition, these mutants showed increased sensitivity to certain ..beta..-lactam antibiotics and sodium dodecyl sulfate, but did not exhibit an increase in sensitivity to other antibiotics and detergents. The nucleotide sequence of these mutants has been determined. In all cases, residue 74 (arginine) of the mature OmpC protein was affected. The results suggest that this region of the OmpC protein is involved in the pore domain and that the alterations lead to an increased pore size.
- Research Organization:
- Princeton Univ., NJ
- OSTI ID:
- 5381307
- Journal Information:
- J. Bacteriol.; (United States), Vol. 170:2
- Country of Publication:
- United States
- Language:
- English
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BACTERIA
METABOLISM
PROTEINS
DNA SEQUENCING
GENETIC MAPPING
ANTIBIOTICS
CARBON 14 COMPOUNDS
MALTOSE
MUTANTS
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SENSITIVITY
TRACER TECHNIQUES
UPTAKE
ANTI-INFECTIVE AGENTS
CARBOHYDRATES
DISACCHARIDES
DRUGS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MAPPING
MICROORGANISMS
OLIGOSACCHARIDES
ORGANIC COMPOUNDS
SACCHARIDES
STRUCTURAL CHEMICAL ANALYSIS
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