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http://purl.uniprot.org/citations/18452539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18452539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18452539http://www.w3.org/2000/01/rdf-schema#comment"The osmotolerant yeast Candida glycerinogenes produces glycerol as a major metabolite on an industrial scale, but the underlying molecular mechanisms are poorly understood. We cloned and characterized a 4900-bp genomic fragment containing the CgGPD gene encoding a glycerol-3-phosphate dehydrogenase homologous to GPD genes in other yeasts using degenerate primers in conjunction with inverse PCR. Sequence analysis revealed a 1167-bp open reading frame encoding a putative peptide of 388 deduced amino acids with a molecular mass of 42 695 Da. The CgGPD gene consisted of an N-terminal NAD(+)-binding domain and a central catalytic domain, whereas seven stress response elements were found in the upstream region. Functional analysis revealed that Saccharomyces cerevisiae gpd1Delta and gpd1Delta/gpd2Delta osmosensitive mutants transformed with CgGPD were restored to the wild-type phenotype when cultured in high osmolarity media, suggesting that it is a functional GPD protein. Transformants also accumulated glycerol intracellularly and GPD-specific activity increased significantly when stressed with NaCl, whereas the S. cerevisiae mutants transformed with the empty plasmid showed only slight increases. The full-length CgGPD gene sequence including upstream and downstream regions has been deposited in GenBank under accession no. EU186536."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.org/dc/terms/identifier"doi:10.1111/j.1567-1364.2008.00382.x"xsd:string
http://purl.uniprot.org/citations/18452539http://purl.org/dc/terms/identifier"doi:10.1111/j.1567-1364.2008.00382.x"xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Rao Z."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Rao Z."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Shen W."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Shen W."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Fang H."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Fang H."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Zhuge J."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Zhuge J."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Zhuge B."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/author"Zhuge B."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/name"FEMS Yeast Res."xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/name"FEMS Yeast Res"xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/pages"725-734"xsd:string
http://purl.uniprot.org/citations/18452539http://purl.uniprot.org/core/pages"725-734"xsd:string