Disease relevance of Gld

• Sequence comparison of Drosophila melanogaster glucose dehydrogenase, Escherichia coli choline dehydrogenase, Aspergillus niger glucose oxidase and Hansenula polymorpha methanol oxidase indicates that these four diverse flavoproteins are homologous, defining a new family of proteins named the GMC oxidoreductases [1].
• The recently determined primary structure of glucose dehydrogenase from Bacillus megaterium was scanned by computerized comparisons for similarities with known polyol and alcohol dehydrogenases [2].
• The results revealed a highly significant similarity between this glucose dehydrogenase and ribitol dehydrogenase from Klebsiella aerogenes [2].
• On the other hand, we observed an increase in the expression of C. capitata Go protein with age, as revealed by pertussis toxin-catalysed ADP-ribosylation and immunoblotting experiments, that was not correlated with an increase in beta subunit levels [3].

High impact information on Gld

• We have isolated the Gld gene and three other functionally related genes in the eclosion gene cluster by the method of chromosome walking [4].
• Isolation of the eclosion gene cluster and the developmental expression of the Gld gene in Drosophila melanogaster [4].
• The temporal and spatial expression of this RNA is correlated with the expression of the GLD enzyme and levels of the steroid hormone ecdysterone [4].
• A conserved palindromic sequence (Gpal) in the promoter region of the Drosophila Gld directs expression of a heterologous reporter gene in transgenic flies to the anterior spiracular glands of third instar larvae and to the ejaculatory bulb of adult males [5].
• A gene fusion composed of the D. melanogaster Gld promoter and the lacZ gene is expressed in the anterior spiracular glands of transgenic larvae [5].

Biological context of Gld

• We report herein that interactions among proximal promoter elements and a cluster of intronically located enhancers and silencers specify the complex regulation of Gld that underlies its diverse functions [6].
• We have precisely mapped and sequenced the three 5' exons of the Drosophila melanogaster Gld gene and have identified the start sites for transcription and translation [7].
• Regulation of Gld in the reproductive organs is particularly complex, involving interactions among the Gpal proximal promoter elements, a unique TATA box, three distinct enhancer types, and one or more silencer elements [6].
• Molecular structure and transformation of the glucose dehydrogenase gene in Drosophila melanogaster [7].
• To initially define the contribution of cis- versus trans-acting factors responsible for differences in adult GLD expression between two of these species--D. melanogaster and D. pseudoobscura--we transferred the D. pseudoobscura Gld to the genome of D. melanogaster and investigated its expression [8].

Anatomical context of Gld

• A model of the evolution of Gld expression in the ejaculatory duct and oviduct is presented [9].
• During metamorphosis Gld is expressed in a variety of tissues derived from the ectoderm [10].

Associations of Gld with chemical compounds

• Premature exposure of wild type mid-third instar larvae to ecdysterone also results in the rapid accumulation of Gld mRNA and signals the repression of Adh mRNA [11].
• In particular, we identified striking changes in gene number or genomic organization for genes encoding glycolytic enzymes, cellulase, glucose oxidase and glucose dehydrogenases, glucose-methanol-choline (GMC) oxidoreductases, fucosyltransferases, and lysozymes [12].

Other interactions of Gld

• In mutant l(3)ecdysone-1ts (ecd-1) larvae, the normal peak of Gld mRNA late in the third instar is not expressed [11].

Analytical, diagnostic and therapeutic context of Gld

• Sequence analysis of the Gld YYRR box in three Drosophila species revealed a high degree of conservation despite its intronic location [13].
• This increase could be attributed in part to an increase in the alpha subunit of the Go-like protein, as revealed by immunoblotting with anti-Go alpha polyclonal antibody [14].
• This substrate, which showed only one isoform when analysed by isoelectric focusing, was recognized by immunoblotting and immunoprecipitation techniques using a polyclonal antibody against the alpha subunit of the Go protein purified from bovine brain and can be thus considered as a Go-like protein [14].
• The results of interspecific genital imaginal disc transplantation experiments indicate that the expanded morphology and GLD expression do not require any species- or sex-specific diffusible factors [15].

References