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Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli.
J Bacteriol 1988; 170(6):2841-9JB

Abstract

It has been shown previously that Escherichia coli accumulates endogenously synthesized trehalose under osmotic stress. We report here that E. coli contained an osmotically regulated trehalose-phosphate synthase which utilized UDP-glucose and glucose 6-phosphate as substrates. In the wild type, the synthase was induced by growth in glucose-mineral medium of elevated osmotic strength and the synthase itself was strongly stimulated by K+ and other monovalent cations. A laboratory strain which expressed the synthase at a high constitutive level was found. GalU mutants, defective in synthesis of UDP-glucose, did not accumulate trehalose. Two genes governing the synthase were identified and named otsA and otsB (osmoregulatory trehalose synthesis). They mapped near 42 min in the flbB-uvrC region. Mutants with an otsA-lacZ or otsB-lacZ operon fusion displayed osmotically inducible beta-galactosidase activity; i.e., the activity was increased fivefold by growth in medium of elevated osmotic strength. Mutants unable to synthesize trehalose (galU, otsA, and otsB) were osmotically sensitive in glucose-mineral medium. But an osmotically tolerant phenotype was restored in the presence of glycine betaine, which also partially repressed the synthesis of synthase in the wild type and of beta-galactosidase in ots-lacZ fusion mutants.

Authors+Show Affiliations

Institute of Fisheries, University of Tromsø, Norway.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3131312

Citation

Giaever, H M., et al. "Biochemical and Genetic Characterization of Osmoregulatory Trehalose Synthesis in Escherichia Coli." Journal of Bacteriology, vol. 170, no. 6, 1988, pp. 2841-9.
Giaever HM, Styrvold OB, Kaasen I, et al. Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. J Bacteriol. 1988;170(6):2841-9.
Giaever, H. M., Styrvold, O. B., Kaasen, I., & Strøm, A. R. (1988). Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. Journal of Bacteriology, 170(6), pp. 2841-9.
Giaever HM, et al. Biochemical and Genetic Characterization of Osmoregulatory Trehalose Synthesis in Escherichia Coli. J Bacteriol. 1988;170(6):2841-9. PubMed PMID: 3131312.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. AU - Giaever,H M, AU - Styrvold,O B, AU - Kaasen,I, AU - Strøm,A R, PY - 1988/6/1/pubmed PY - 1988/6/1/medline PY - 1988/6/1/entrez SP - 2841 EP - 9 JF - Journal of bacteriology JO - J. Bacteriol. VL - 170 IS - 6 N2 - It has been shown previously that Escherichia coli accumulates endogenously synthesized trehalose under osmotic stress. We report here that E. coli contained an osmotically regulated trehalose-phosphate synthase which utilized UDP-glucose and glucose 6-phosphate as substrates. In the wild type, the synthase was induced by growth in glucose-mineral medium of elevated osmotic strength and the synthase itself was strongly stimulated by K+ and other monovalent cations. A laboratory strain which expressed the synthase at a high constitutive level was found. GalU mutants, defective in synthesis of UDP-glucose, did not accumulate trehalose. Two genes governing the synthase were identified and named otsA and otsB (osmoregulatory trehalose synthesis). They mapped near 42 min in the flbB-uvrC region. Mutants with an otsA-lacZ or otsB-lacZ operon fusion displayed osmotically inducible beta-galactosidase activity; i.e., the activity was increased fivefold by growth in medium of elevated osmotic strength. Mutants unable to synthesize trehalose (galU, otsA, and otsB) were osmotically sensitive in glucose-mineral medium. But an osmotically tolerant phenotype was restored in the presence of glycine betaine, which also partially repressed the synthesis of synthase in the wild type and of beta-galactosidase in ots-lacZ fusion mutants. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/3131312/Biochemical_and_genetic_characterization_of_osmoregulatory_trehalose_synthesis_in_Escherichia_coli_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=3131312 DB - PRIME DP - Unbound Medicine ER -