Trehalose accumulation in a high-trehalose-accumulating mutant of Saccharomycopsis fibuligera sdu does not respond to stress treatments

Lu, Liang; Wang, X. K.; Zhu, Kailing; M., Z.

doi:10.1134/s0006297906120017

Cited by 4 publications

(3 citation statements)

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“…Properties of the participating enzymes in trehalose synthesis have been studied in Pseudomonas (Ohguchi et al , 1997; Ma et al , 2006), Mycobacterium (Klutts et al , 2003; Pan et al , 2004), archaebacteria (Nakada et al , 1996), Saccharomycopsis fibuligera (Liang et al , 2006), Selaginella (Valenzuela-Soto et al , 2004; Márquez-Escalante et al , 2006) and the amoeba Dictyostelium discoideum (Killick, 1979). Genes of TPS have been characterized in a number of organisms representing many different systematic groups, from bacteria, yeasts, insects, nematodes and crabs, to plants (De Virgilio et al , 1993; Kaazen et al , 1994; Vogel et al , 2001; Chen et al , 2002, Pellerone et al , 2003; Chung, 2008).…”

Section: Introductionmentioning

confidence: 99%

Purification and partial biochemical–genetic characterization of trehalose 6-phosphate synthase from muscles of adult femaleAscaris suum

et al. 2012

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AbstractTrehalose 6-phosphate (T6P) synthase (TPS;EC2.4.1.15) was isolated from muscles ofAscaris suumby ammonium sulphate fractionation, ion-exchange DEAE SEPHACELTManion exchanger column chromatography and Sepharose 6B gel filtration. On sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE), 265-fold purified TPS exhibited a molecular weight of 66 kDa. The optimum pH and temperature of the purified enzyme were 3.8–4.2 and 35°C, respectively. The isoelectric point (pI) of TPS was pH 5.4. The studied TPS was not absolutely substrate specific. Besides glucose 6-phosphate, the enzyme was able to use fructose 6-phosphate as an acceptor of glucose. TPS was activated by 10 mMMgCl2, 10 mMCaCl2and 10 mMNaCl. In addition, it was inhibited by ethylenediaminetetra-acetic acid (EDTA), KCl, FeCl3and ZnCl2. Two genes encoding TPS were isolated and sequenced from muscles of the parasite. Complete coding sequences fortps1(JF412033.2) andtps2(JF412034.2) were 3917 bp and 3976 bp, respectively. Translation products (AEX60788.1 and AEX60787.1) showed expression to the glucosyltransferase-GTB-type superfamily.

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Section: Introductionmentioning

confidence: 99%

Purification and partial biochemical–genetic characterization of trehalose 6-phosphate synthase from muscles of adult femaleAscaris suum

et al. 2012

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“…CODEHOP PCR is efficient in designing degenerate primers and has been successfully utilized for cloning short homogenous genes from distant related organisms as diverse as fish, frog, protozoa, plants, viruses and bacteria (Rose et al, 2003, Liang et al, 2006Luzhetskyy et al, 2007). TAIL PCR is an available way for genomic walking.…”

Section: Discussionmentioning

confidence: 99%

Evidence for horizontal gene transfer of a tetrahydrofuran monooxygenase: Cloning and analysis of a gene cluster for tetrahydrofuran degradation in Rhodococcus sp. YYL

Yao¹,

Lü²,

Zhu³

et al. 2013

Afr. J. Microbiol. Res.

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A gene cluster encoding tetrahydrofuran (THF) degrading related enzymes was first isolated from Rhodococcus sp. YYL, a strain of the genus Rhodococcus, which was first reported to degrade tetrahydrofuran, by combination of COnsensus-DEgenerate Hybrid oligonucleotide Primer PCR and thermal asymmetric interlaced PCR. Sequence analysis of the gene cluster revealed 9 open reading frames containing genes encoding a Rhodococcus sp. YYL multiple component tetrahydrofuran monooxygenase. The tetrahydrofuran monooxygenase genes had similarities higher than 92% with these in Pseudonocardia sp. K1, but had low similarities with other monooxygenase genes using BLAST search in GenBanK. The high specific of tetrahydrofuran monooxygenase genes was further proved by PCR amplification of no product using genomic DNA of other bacteria or even activated sludge as template with primers targeting at the α-subunit of this monooxygenase. Phylogenetic analysis based on amino acid sequences and 16S rDNA strongly suggested that this monooxygenase occurred by horizontal gene transfer. Base composition analysis and the existence of a transposase gene in the gene cluster further proposed that this monooxygenase originated from the genus Rhodococcus and it might be transformed by a transposon between different species.

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“…In baker s yeast, TPS1 transcription is induced by ethanol stress (Liang et al, 2006). We investigated by Northern hybridization whether TPS1 transcription in IB1304 cells was also induced under ethanol stress conditions.…”

Section: Msn2 and Msn4 Are Required For The Formation Of High Levels mentioning

confidence: 99%

Mechanism of high trehalose accumulation in a spore clone isolated from Shirakami kodama yeast

Nakazawa

Obata

Ito

et al. 2014

J. Gen. Appl. Microbiol.

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The intracellular trehalose levels in Shirakami kodama yeast, a strain of Saccharomyces cerevisiae, isolated in 1997 from leaf mold in the Shirakami Mountains and since used as a commercial baker s yeast, are remarkably high, which presumably is related to its tolerance of freezing and drought conditions. We isolated a spore clone from Shirakami kodama yeast with about 1.7-fold higher intracellular trehalose levels than the parental strain and set out to elucidate how this spore clone can accumulate intracellular trehalose to such a high concentration. The gene for trehalose 6-phosphate synthase, TPS1, was duplicated in this spore clone. Both TPS1 genes contributed to the high level of intracellular trehalose as a 3.4-fold decrease resulted from the disruption of one of the two TPS1 genes. Both Msn2 and Msn4, which bind to stress responsive elements in the promoter region of TPS1, were required for production of high levels of trehalose. Furthermore, the neutral trehalase activity of this spore clone is about 3-fold less than that of the laboratory strain although the gene for neutral trehalase, NTH1, functioned normally. These findings indicate that two TPS1 genes and the low trehalase activity are associated with high trehalose accumulation in this spore clone. The wide range of stresses of which we found the spore clone to be tolerant makes this yeast very attractive for commercial application and for further research into the mechanisms underlying stress responses and trehalose metabolism.Key words: NTH1; TPS1; trehalase; trehalose; Shirakami kodama yeast IntroductionThe disaccharide trehalose is found in organisms as diverse as yeast and other fungi, bacteria, and a variety of plants and invertebrates, in which it accumulates significantly during adverse environmental conditions (Gaff, 1971;Thevelein, 1984;Singer and Lindqust, 1998;Zentella et al., 1999;Chen et al., 2002;Schluepmann et al., 2004). A number of studies have demonstrated a correlation between intracellular trehalose levels and the ability of Saccharomyces cerevisiae to survive various environmental stresses, such as starvation, desiccation, dehydration, osmotic and oxidative stress and extremes in temperature (Thevelein and Hohmann, 1995;Hounsa et al., 1998;Elbein et al., 2003;Herdeiro et al., 2006).In S. cerevisiae, the enzymes that catalyze the reactions of trehalose biosynthesis, a trehalose 6-phosphate (T6P) synthase encoded by TPS1 and a T6P phosphatase encoded by TPS2, are part of a complex in which two other, non-catalytic proteins, Tsl1 and Tps3, participate (Gancedo and Flores, 2004). Degradation of cytoplasmic trehalose is mainly catalyzed by neutral trehalases that work best at pH 6.8 7.0 (Londesborough and Varimo, 1984;App and Holzer, 1989) and are encoded by two duplicated genes, NTH1 and NTH2, which share 77% identity in their predicted amino acid sequences (Kopp et al., 1993(Kopp et al., , 1994Wolf and Lohan, 1994). Major trehalase activity for intracellular trehalose is conferred by NTH1, the expression of which is regulated by...

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Trehalose accumulation in a high-trehalose-accumulating mutant of Saccharomycopsis fibuligera sdu does not respond to stress treatments

Cited by 4 publications

References 16 publications

Purification and partial biochemical–genetic characterization of trehalose 6-phosphate synthase from muscles of adult femaleAscaris suum

Purification and partial biochemical–genetic characterization of trehalose 6-phosphate synthase from muscles of adult femaleAscaris suum

Evidence for horizontal gene transfer of a tetrahydrofuran monooxygenase: Cloning and analysis of a gene cluster for tetrahydrofuran degradation in Rhodococcus sp. YYL

Mechanism of high trehalose accumulation in a spore clone isolated from Shirakami kodama yeast

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