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2000•FEMS Microbiology LettersOpen access

A colicin-tolerantEscherichia colimutant that confers Hfl phenotype carries two mutations in the region coding for the C-terminal domain of FtsH (HflB)

Dinah Teff, Simi Koby, Yoram Shotland, Teru Ogura, Amos B. Oppenheim

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Abstract

An Escherichia coli mutant, ER437, which was originally isolated for colicin tolerance, was found to carry two amino acid changes in the C-terminal portion of FtsH (HflB). These mutations were demonstrated to reduce the ability of FtsH to degrade the phage lambda CII protein in vivo and in vitro, providing a rationalization for the mutant Hfl phenotype.

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An Escherichia coli mutant, ER437, which was originally isolated for colicin tolerance, was found to carry two amino acid changes in the C-terminal portion of FtsH (HflB). These mutations were demonstrated to reduce the ability of FtsH to degrade the phage lambda CII protein in vivo and in vitro, providing a rationalization for the mutant Hfl phenotype.

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Available abstract

An Escherichia coli mutant, ER437, which was originally isolated for colicin tolerance, was found to carry two amino acid changes in the C-terminal portion of FtsH (HflB). These mutations were demonstrated to reduce the ability of FtsH to degrade the phage lambda CII protein in vivo and in vitro, providing a rationalization for the mutant Hfl phenotype.

Key concepts: Colicin, Mutant, Phenotype, Escherichia coli, Genetics, Biology, Coding region, Mutation

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A colicin-tolerantEscherichia colimutant that confers Hfl phenotype carries two mutations in the region coding for the C-terminal domain of FtsH (HflB) — Research Paper | ScholarLens