Isolation and characterization of OmpC porin mutants with altered pore properties
Description
The LamB protien is normally required for the uptake of maltodextrins. Starting with a LamB- OmpF- strain, we have isolated mutants that will grow on maltodextrins. The mutation conferring the Dex+ phenotype in the majority of these mutants has been mapped to the ompC locus. These mutants, unlike LamB- OmpF- strains, grew on maltotriose and maltotetraose, but not on maltopentaose, and showed a significantly higher rate of [14C] maltose uptake than the parent strain did. In addition, these mutants showed increased sensitivity to certain β-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
Additional details
Publishing Information
- Journal Title
- J. Bacteriol.
- Journal Volume
- 170
- Journal Issue
- 2
- Series
- J. Bacteriol.
- Journal Page Range
- 528-533
- ISSN
- 0021-9193
- CODEN
- JOBAA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 19063018
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- ANTIBIOTICS; BACTERIA; CARBON 14 COMPOUNDS; DNA SEQUENCING; GENETIC MAPPING; MALTOSE; METABOLISM; MUTANTS; PHENOTYPE; PROTEINS; SENSITIVITY; TRACER TECHNIQUES; UPTAKE
- Descriptors DEC
- CARBOHYDRATES; CARBON COMPOUNDS; DISACCHARIDES; DRUGS; ISOTOPE APPLICATIONS; MICROORGANISMS; OLIGOSACCHARIDES; ORGANIC COMPOUNDS; SACCHARIDES; STRUCTURAL CHEMICAL ANALYSIS