{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T02:20:53Z","timestamp":1776910853527,"version":"3.51.2"},"reference-count":45,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2006,10,27]],"date-time":"2006-10-27T00:00:00Z","timestamp":1161907200000},"content-version":"vor","delay-in-days":4957,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[1993,4]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Endogenously synthesized trehalose is a stress protectant in <jats:italic>Escherichia coli.<\/jats:italic> 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\u2010phaseinduced heat tolerance. Mechanisms for stress protection by trehalose are discussed. The genes for trehalose\u20106\u2010phosphate synthase (<jats:italic>otsA<\/jats:italic>) and anabolic trehalose\u20106\u2010phosphate phosphatase (<jats:italic>otsB<\/jats:italic>) 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 <jats:italic>rpoS (katF). rpoS<\/jats:italic> is amber\u2010mutated in <jats:italic>E. coli<\/jats:italic> K\u201012 and its DNA sequence varies among K\u201012 strains. For trehalose catabolism under osmotic stress <jats:italic>E. coli<\/jats:italic> depends on the osmoticcally inducible periplasmic trehalase (TreA). In the absence of osmotic stress, trehalose induces the formation of an enzyme II<jats:sup>Tre<\/jats:sup> (TreB) of the group translocation system, a catabolic trehalose\u20106\u2010phosphate phosphatase (TreE), and an amylotrehalase (TreC) which converts trehalose to free glucose and a glucose polymer.<\/jats:p>","DOI":"10.1111\/j.1365-2958.1993.tb01564.x","type":"journal-article","created":{"date-parts":[[2006,10,28]],"date-time":"2006-10-28T01:23:06Z","timestamp":1161998586000},"page":"205-210","source":"Crossref","is-referenced-by-count":309,"title":["Trehalose metabolism in <i>Escherichia coli<\/i>: stress protection and stress regulation of gene expression"],"prefix":"10.1111","volume":"8","author":[{"given":"A. 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