Isolation and characterization of OmpC porin mutants with altered pore properties.

Rajeev Misra, S. A. Benson

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

The LamB protein 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 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.

Original languageEnglish (US)
Pages (from-to)528-533
Number of pages6
JournalJournal of Bacteriology
Volume170
Issue number2
StatePublished - Feb 1988
Externally publishedYes

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Porins
Anti-Bacterial Agents
Maltose
beta-Lactams
Sodium Dodecyl Sulfate
Detergents
Arginine
Phenotype
Mutation
Proteins
OmpC protein
maltodextrin
maltotetraose
maltotriose
maltopentaose

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Isolation and characterization of OmpC porin mutants with altered pore properties. / Misra, Rajeev; Benson, S. A.

In: Journal of Bacteriology, Vol. 170, No. 2, 02.1988, p. 528-533.

Research output: Contribution to journalArticle

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