Disease relevance of ADH1

• We show that AtMYB2 is induced by hypoxia with kinetics compatible with a role in the regulation of ADH1 [1].
• In the Arabidopsis alcohol dehydrogenase (Adh) promoter, the G-box regulates expression in response to cold and dehydration, presumably through the action of abscisic acid (ABA), and is bound by a nuclear protein complex in vivo during expression in cell cultures [2].
• Here, wheat TaPCS1 cDNA expression was either targeted to Arabidopsis roots with the Arabidopsis alcohol dehydrogenase (Adh) promoter (Adh::TaPCS1/cad1-3) or ectopically expressed with the cauliflower mosaic virus 35S promoter (35S::TaPCS1/cad1-3) in the PC-deficient mutant cad1-3 [3].
• The arabidopsis ADH (alcohol dehydrogenase) locus was mobilized from Agrobacterium, and integration into the recipient genome was studied [4].

High impact information on ADH1

• This region, which contains DNA sequences I, G and GT boxes, with homology to other ribulose-1,5-bisphosphate carboxylase small subunit (RBCS) gene promoter sequences, directed expression independent of orientation and relative position in the Adh promoter [5].
• Site-specific mutagenesis of these conserved sequences and subsequent expression analysis in transgenic tobacco showed that both G box and I box mutations in the context of the full (-1700 to +21) rbcS-1A promoter substantially reduced the expression of Adh and beta-glucuronidase (GUS) reporter genes [5].
• By contrast, a Ds insertion mutant of the AtMYC2 gene was less sensitive to ABA and showed significantly decreased ABA-induced gene expression of rd22 and AtADH1 [6].
• The ABA-induced gene expression of rd22 and AtADH1 was enhanced in these transgenic plants [6].
• ZmABI4 also binds to the promoter of the sugar-responsive ADH1 gene, demonstrating the ability of this protein to regulate both ABA- and sugar-regulated pathways [7].

Chemical compound and disease context of ADH1

• Our results indicate that, although induction of the Adh gene by ABA, dehydration, and low temperature required the same cis-acting promoter elements, their regulatory pathways were at least partially separated in a combined dehydration/ABA pathway and an ABA-independent low-temperature pathway [8].
• Therefore, we conclude that ethylene is needed, but not sufficient for, the induction of ADH in Arabidopsis during hypoxia [9].
• These changes in ADH could be induced either by spaceflight hypoxia resulting from inhibition of gravity mediated O2 transport, or by a non-specific stress response due to inhibition of gravisensing [10].

Biological context of ADH1

• The DNA sequence contains an open reading frame capable of encoding a polypeptide the same length as maize ADH1 and ADH2 (379 amino acids) and having approximately equal to 80% homology with both maize enzymes [11].
• For mutant R002, which does not contain any detectable levels of ADH protein and mRNA, we have found that the mutation is due to a single C to T base pair substitution in the reading frame; this leads to the incorporation of a TAG stop codon (amber nonsense mutation) [12].
• This gives rise to a Cys to Tyr amino acid substitution in the active site of the ADH enzyme [12].
• The last, L6, is an unknown gene close to ALCOHOL DEHYDROGENASE on chromosome 1 [13].
• Adh is expressed in non-green tissue, induced by anaerobiosis, and repressed in leaves [14].

Anatomical context of ADH1

• When driven by a constitutive promoter, AtMYB2 is able to transactivate ADH1 expression in transient assays in both Arabidopsis and Nicotiana plumbaginifolia protoplasts, and in particle bombardment of Pisum sativum leaves [1].
• The alcohol dehydrogenase gene (NtADH) was previously isolated from tobacco BY2 suspension cultured cell [15].

Associations of ADH1 with chemical compounds

• We found that the hypoxic induction of ADH can be partially inhibited by aminooxy acetic acid, an inhibitor of ethylene biosynthesis [9].
• Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis [8].
• The T-DNA targeting construct contained two flanking regions of the target alcohol dehydrogenase gene as homologous sequences, and neomycin phosphotransferase and cytosine deaminase as positive and negative markers, respectively [16].
• These results suggest that these ethanol-resistant mutants are impaired in one of the structural genes coding for alcohol dehydrogenase [17].
• Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class p and liver class I alcohol dehydrogenases [18].

Physical interactions of ADH1

• The transcription factor AtMYB2 binds to two sequence motifs in the promoter of the Arabidopsis ADH1 gene [1].

Analytical, diagnostic and therapeutic context of ADH1

• Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene [11].
• We report here that in vitro Adh G-box binding activity is present in crude whole cell extracts of both cell culture and leaves of Arabidopsis [14].
• Northern blot, RT-PCR, and Western blot analyses showed Adh promoter-driven TaPCS1 expression only in roots and thus demonstrated lack of long-distance TaPCS1 mRNA and protein transport in plants [3].
• A short segment of the pea Adh promoter region (-290 to +57) was fused to a reporter gene and introduced into protoplasts of Nicotiana plumbaginifolia by electroporation [19].
• Plants were monitored in vivo during exposure to hypoxia, high salt, cold, and abcissic acid in experiments designed to characterize the utility and responses of the Adh/GFP biosensors [20].

References