Enzymatic control of anhydrobiosis-related accumulation of trehalose in the sleeping chironomid, Polypedilum vanderplanki.
Bottom Line: Although computational prediction indicated that the alternative splicing variants (PvTpsα/β) obtained encoded probable functional motifs consisting of a typical consensus domain of TPS and a conserved sequence of TPP, PvTpsα did not exert activity as TPP, but only as TPS.The translated product of the TREH ortholog (PvTreh) certainly degraded trehalose to glucose.Trehalose was synthesized abundantly, consistent with increased activities of TPS and TPP and suppressed TREH activity.
Affiliation: Anhydrobiosis Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.Show MeSH
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Mentions: In addition to its role as an anhydroprotectant, trehalose is generally known as a carbon and energy source for bacteria and yeast . In bacteria and yeast, trehalose is synthesized from glucose-6-phosphate and UDP-glucose, catalyzed by trehalose-6-phosphate synthase (TPS; EC 22.214.171.124) and trehalose-6-phosphate phosphatase (TPP; EC 126.96.36.199), and the relevant genes have been cloned and well characterized (Fig. 1A). This synthetic pathway is considered to be conserved in a wide range of taxa, including unicellular and multicellular organisms, because these genes have been found in algae, fungi, plants and invertebrates .
Affiliation: Anhydrobiosis Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.