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Trehalose metabolism in Escherichia coli : stress protection and stress regulation of gene expression
Author(s) -
Strom A. R.,
Kaasen I.
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01564.x
Subject(s) - trehalose , rpos , biology , biochemistry , trehalase , escherichia coli , osmotic shock , osmoprotectant , sigma factor , catabolism , phosphatase , enzyme , gene expression , gene , proline , amino acid , promoter , rna polymerase
Summary Endogenously synthesized trehalose is a stress protectant in Escherichia coli. Externally supplied trehalose does not serve as a stress protectant, but it can be utilized as the sole source of carbon and energy. Mutants defective in trehalose synthesis display an impaired osmotic tolerance in minimal growth media without glycine betaine, and an impaired stationary‐phaseinduced heat tolerance. Mechanisms for stress protection by trehalose are discussed. The genes for trehalose‐6‐phosphate synthase ( otsA ) and anabolic trehalose‐6‐phosphate phosphatase ( otsB ) constitute an operon. Their expression is induced both by osmotic stress and by growth into the stationary phase and depend on the sigma factor encoded by rpoS (katF). rpoS is amber‐mutated in E. coli K‐12 and its DNA sequence varies among K‐12 strains. For trehalose catabolism under osmotic stress E. coli depends on the osmoticcally inducible periplasmic trehalase (TreA). In the absence of osmotic stress, trehalose induces the formation of an enzyme II Tre (TreB) of the group translocation system, a catabolic trehalose‐6‐phosphate phosphatase (TreE), and an amylotrehalase (TreC) which converts trehalose to free glucose and a glucose polymer.