Cloning and characterization of a TEF gene for elongation factor 1? from the yeast Arxula adeninivorans

Rösel, Harald; Kunze, Gotthard

doi:10.1007/bf00326434

Cited by 42 publications

(30 citation statements)

References 26 publications

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“…In Northern hybridizations, levels of the ATAN1 transcript were assessed in comparison to those of the constitutively expressed TEF1 RNA (Rösel and Kunze, 1995). Total RNA was extracted from the wild-type strain LS3 that had been grown as budding cells for 48 h at 30 • C in YMM supplemented with 2% glucose, and subsequently shifted to YMM supplemented with 0.5% glucose, tannic acid or gallic acid as carbon source.…”

Section: Carbon Source-dependent Expression Of the Atan1 Genementioning

confidence: 99%

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Böer¹,

Bode²,

Mock³

et al. 2009

Yeast

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The tannase-encoding Arxula adeninivorans gene ATAN1 was isolated from genomic DNA by PCR, using as primers oligonucleotide sequences derived from peptides obtained after tryptic digestion of the purified tannase protein. The gene harbours an ORF of 1764 bp, encoding a 587-amino acid protein, preceded by an N-terminal secretion sequence comprising 28 residues. The deduced amino acid sequence was similar to those of tannases from Aspergillus oryzae (50% identity), A. niger (48%) and putative tannases from A. fumigatus (52%) and A. nidulans (50%). The sequence contains the consensus pentapeptide motif (-Gly-X-Ser-X-Gly-) which forms part of the catalytic centre of serine hydrolases. Expression of ATAN1 is regulated by the carbon source. Supplementation with tannic acid or gallic acid leads to induction of ATAN1, and accumulation of the native tannase enzyme in the medium. The enzymes recovered from both wild-type and recombinant strains were essentially indistinguishable. A molecular mass of ∼320 kDa was determined, indicating that the native, glycosylated tannase consists of four identical subunits. The enzyme has a temperature optimum at 35-40• C and a pH optimum at ∼6.0. The enzyme is able to remove gallic acid from both condensed and hydrolysable tannins. The wildtype strain LS3 secreted amounts of tannase equivalent to 100 U/l under inducing conditions, while the transformant strain, which overexpresses the ATAN1 gene from the strong, constitutively active A. adeninivorans TEF1 promoter, produced levels of up to 400 U/l when grown in glucose medium in shake flasks.

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Section: Carbon Source-dependent Expression Of the Atan1 Genementioning

confidence: 99%

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Böer¹,

Bode²,

Mock³

et al. 2009

Yeast

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“…RNA was hybridized under high stringency conditions at 42°C as recommended by the NEN Research Products (USA) instructions manual for GeneScreen nylon membranes. Chromosomal DNA fragments of the glucoamylase (GAA) and TEF1 genes from A. adeninivorans LS3 (Rösel and Kunze 1995;Bui et al 1996a) were used as radioactive DNA probes (Stoltenburg et al 1995).…”

Section: Enzyme Assaymentioning

confidence: 99%

“…To analyse catabolite repression in more detail, the glucoamylase mRNA and protein levels of all three A. adeninivorans cultures were determined by Northern hy- (Rösel and Kunze 1995) was used as a control. The TEF1 transcript level was constant for the most part during cultivation in all three cultures, but varied after 45 h for both LS3-30°C and 135-30°C.…”

Section: Is Protein Biosynthesis Influenced By Dimorphism?mentioning

confidence: 99%

Morphology-related effects on gene expression and protein accumulation of the yeast Arxula adeninivorans LS3

Wartmann

Erdmann

Kunze

et al. 2000

Archives of Microbiology

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The dimorphism of the yeast Arxula adeninivorans LS3 is regulated by cultivation temperatures. Up to 42 degrees C the yeast grows as budding cells, which turn to mycelia at higher temperatures. To test whether the dimorphism is exclusively induced by high temperatures or also by other conditions, mutants were selected with an altered behaviour with respect to dimorphism. After mutagenesis with N-methyl-N'-nitro-N-nitrosoguanidine, five of 25,000 colonies formed a very rough surface consisting of mycelia at 30 degrees C, in contrast to the wild-type. These mutants allow temperature-mediated and morphology-related effects on gene expression and protein accumulation to be distinguished. Budding cells and mycelia showed different expression of genes encoding secretory proteins at the same temperature. Mycelia secreted two-fold more protein than budding cells, including the enzymes glucoamylase and invertase. This indicated that morphology, rather than temperature, is the decisive factor in the analysed processes.

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“…Polyadenylation occurred at a site ϳ55 bp after the stop codon. At the DNA level, BLAST analysis of CnTEF1 indicated that the most highly related TEF1 genes sequenced to date were from the yeast Arxula adeninivorans (Rosel and Kunze, 1995) and the filamentous fungus Ashbya gossypii (Steiner and Philippsen, 1994).…”

Section: Cloning and Nucleotide Sequence Analysis Of A Cdna Copy Of Cmentioning

confidence: 99%

Cloning and Molecular Characterization ofCnTEF1Which Encodes Translation Elongation Factor 1α inCryptococcus neoformans

Thornewell

Peery

Skatrud

1997

Fungal Genetics and Biology

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Cloning and characterization of a TEF gene for elongation factor 1? from the yeast Arxula adeninivorans

Cited by 42 publications

References 26 publications

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Morphology-related effects on gene expression and protein accumulation of the yeast Arxula adeninivorans LS3

Cloning and Molecular Characterization ofCnTEF1Which Encodes Translation Elongation Factor 1α inCryptococcus neoformans

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