Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter sp. Q36

Maruta, Kazuhiko; Hattori, Katsuji; Nakada, Tetsuya; Kubota, Michio; Sugimoto, Toshiyuki; Kurimoto, Masashi

doi:10.1016/0304-4165(95)00139-5

Cited by 80 publications

(48 citation statements)

References 16 publications

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“…In the first step, maltooligosyltrehalose synthase (TreY) catalyzes the convertion of maltopentaose into maltooligosyl trehalose by intramolecular transglycosylation, and in the second step, maltooligosyltrehalose trehalohydrolase (TreZ) hydrolizes the maltooligosyl trehalose, releasing free trehalose (Maruta et al, 1995). This pathway is also found in other bacterial species such as Rhizobium (Maruta et al, 1996a), Bradyrhizobium japonicum (Sugawara et al, 2010) and Corynebacterium (Tzvetkov et al, 2003), but is missing in other major bacterial groups including E. coli and Bacillus subtilis. Archaea Sulfolobus also uses this pathway for trehalose synthesis (Maruta et al, 1996b).…”

Section: Trey-trez Pathwaymentioning

confidence: 96%

Trehalose and Abiotic Stress in Biological Systems

Iordăchescu¹,

Imai²

2011

Abiotic Stress in Plants - Mechanisms and Adaptations

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Section: Trey-trez Pathwaymentioning

confidence: 96%

Trehalose and Abiotic Stress in Biological Systems

Iordăchescu¹,

Imai²

2011

Abiotic Stress in Plants - Mechanisms and Adaptations

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“…Lactoylgluthation lyase, fosphomicin resistance protein (130). Among the proteins associated with oxidative stress response, Deinococcus encodes three catalases (DR1998, DRA0259, and DRA0146), two of which are highly similar to one another and to catalases from other bacteria whereas the third is only distantly related to other catalases.…”

Section: Dra0145mentioning

confidence: 99%

Genome of the Extremely Radiation-Resistant Bacterium Deinococcus radiodurans Viewed from the Perspective of Comparative Genomics

Makarova

Aravind

Wolf

et al. 2001

Microbiol Mol Biol Rev

656

612

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The bacterium Deinococcus radiodurans shows remarkable resistance to a range of damage caused by ionizing radiation, desiccation, UV radiation, oxidizing agents, and electrophilic mutagens. D. radiodurans is best known for its extreme resistance to ionizing radiation; not only can it grow continuously in the presence of chronic radiation (6 kilorads/h), but also it can survive acute exposures to gamma radiation exceeding 1,500 kilorads without dying or undergoing induced mutation. These characteristics were the impetus for sequencing the genome of D. radiodurans and the ongoing development of its use for bioremediation of radioactive wastes. Although it is known that these multiple resistance phenotypes stem from efficient DNA repair processes, the mechanisms underlying these extraordinary repair capabilities remain poorly understood. In this work we present an extensive comparative sequence analysis of the Deinococcus genome. Deinococcus is the first representative with a completely sequenced genome from a distinct bacterial lineage of extremophiles, the Thermus-Deinococcus group. Phylogenetic tree analysis, combined with the identification of several synapomorphies between Thermus and Deinococcus, supports the hypothesis that it is an ancient group with no clear affinities to any of the other known bacterial lineages. Distinctive features of the Deinococcus genome as well as features shared with other free-living bacteria were revealed by comparison of its proteome to the collection of clusters of orthologous groups of proteins. Analysis of paralogs in Deinococcus has revealed several unique protein families. In addition, specific expansions of several other families including phosphatases, proteases, acyltransferases, and Nudix family pyrophosphohydrolases were detected. Genes that potentially affect DNA repair and recombination and stress responses were investigated in detail. Some proteins appear to have been horizontally transferred from eukaryotes and are not present in other bacteria. For example, three proteins homologous to plant desiccation resistance proteins were identified, and these are particularly interesting because of the correlation between desiccation and radiation resistance. Compared to other bacteria, the D. radiodurans genome is enriched in repetitive sequences, namely, IS-like transposons and small intergenic repeats. In combination, these observations suggest that several different biological mechanisms contribute to the multiple DNA repair-dependent phenotypes of this organism

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“…Homologues of treS are known in some bacteria, including T. thermophilus (Tsusaki et al 1996(Tsusaki et al , 1997White et al 1999;De Smet et al 2000;Wolf et al 2003). A third pathway is found in several bacteria (Maruta et al 1995(Maruta et al , 1996aDe Smet et al 2000) and the hyperthermophilic archaeon Sulfolobus acidocaldarius (Maruta et al 1996c). This pathway uses polyglucose to generate trehalose via maltooligosyltrehalose (MOT) synthase encoded by treY and by MOT trehalohydrolase encoded by treZ.…”

Section: Introductionmentioning

confidence: 99%

Trehalose biosynthesis in Thermus thermophilus RQ-1: biochemical properties of the trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase

2004

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The genes for trehalose synthesis in Thermus thermophilus RQ-1, namely otsA [trehalose-phosphate synthase (TPS)], otsB [trehalose-phosphate phosphatase (TPP)], and treS [trehalose synthase (maltose converting) (TreS)] genes are structurally linked. The TPS/TPP pathway plays a role in osmoadaptation, since mutants unable to synthesize trehalose via this pathway were less osmotolerant, in trehalose-deprived medium, than the wild-type strain. The otsA and otsB genes have now been individually cloned and overexpressed in Escherichia coli and the corresponding recombinant enzymes purified. The apparent molecular masses of TPS and TPP were 52 and 26 kDa, respectively. The recombinant TPS utilized UDP-glucose, TDP-glucose, ADP-glucose, or GDPglucose, in this order as glucosyl donors, and glucose-6-phosphate as the glucosyl acceptor to produce trehalose-6-phosphate (T6P). The recombinant TPP catalyzed the dephosphorylation of T6P to trehalose. This enzyme also dephosphorylated G6P, and this activity was enhanced by NDP-glucose. TPS had an optimal activity at about 98°C and pH near 6.0; TPP had a maximal activity near 70°C and at pH 7.0. The enzymes were extremely thermostable: at 100°C, TPS had a half-life of 31 min, and TPP had a half-life of 40 min. The enzymes did not require the presence of divalent cations for activity; however, the presence of Co 2+ and Mg 2+stimulates both TPS and TPP. This is the first report of the characterization of TPS and TPP from a thermophilic organism.

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Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter sp. Q36

Cited by 80 publications

References 16 publications

Trehalose and Abiotic Stress in Biological Systems

Trehalose and Abiotic Stress in Biological Systems

Genome of the Extremely Radiation-Resistant Bacterium Deinococcus radiodurans Viewed from the Perspective of Comparative Genomics

Trehalose biosynthesis in Thermus thermophilus RQ-1: biochemical properties of the trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase

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