Coenzyme I

Chenopodium quinoa is an emerging halophyte plant that has gained significant attention from researchers in recent years due to its high nutritional value and resilience to environmental stress. This plant serves as an excellent substitute for rice and wheat. However, there has been limited research on it, leaving many of its genes still unidentified. The objective of this research was to identify gene patterns and conduct a bioinformatics analysis across various fields. The expression sequence of the betaine aldehyde dehydrogenase (BADH) gene was predicted using bioinformatics software such as PlantCARE and PlantPan. The findings indicated that different cultivars provide valuable information regarding resistance to the binding sites of MYB transcription factors, hormone response regions, and both promoter and enhancer regions, which contain 32 cis-regulatory elements. This emphasized the role of the BADH gene in responding to abiotic stress. Additionally, the research revealed that the BADH gene activates oxidoreductase activity across different cultivars, influencing NAD or NADP receptors that contribute to stress resistance. The protein lengths identified were 454 and 500 amino acids, respectively. Chloroplast analysis revealed that the GC content for the BADH gene was 37%. From this analysis, it was determined that out of 128 distinct functional genes in the genome, approximately 84 are protein-coding genes. An examination of the domains and motifs in the target genes showed that they contain two conserved sequences: Aldedh and DUF1487. Furthermore, miRNA analysis and promoter investigations indicated that the BADH gene plays a vital role in activating processes related to arginase, protein kinases, superoxide dismutase, tubulins, and membrane proteins. The gene is also crucial for activating nuclear transcription factors through receptor activation. In conclusion, the results suggest that BADH genes contribute to the plant's resistance to salt stress through various mechanisms. Stress acts as a trigger for the activation of this gene, effectively safeguarding the plant against the detrimental effects of environmental stresses.

Fructose-1,6-bisphosphate aldolase (FBA) stands as a pivotal enzyme involved within the Calvin cycle and glycolytic pathways in bacteria and higher plants, but the specific function of OsFBA in rice is still unclear. Here, we identified a chloroplast and mitochondria dual-localized FBA protein, OsFBA1, in rice. Experimental evidence showed that the functionally deficient osfba1 mutants featured a notable decline in chlorophyll content, photosynthetic rate, and severe growth impediment by the three-leaf stage, leading to eventual plant demise. Up-regulation of photosynthetic-pathway genes in the osfba1 mutants indicated the essential role of OsFBA1 in chloroplast development and suggested a compensatory mechanism of other genes in the process. Furthermore, the absence of OsFBA1 impaired the carbon assimilation in young rice seedlings, and supplying exogenous glucose could partially sustain the survival of osfba1 mutant for a few more days. Pathway-specific metabolomics analysis revealed a systemic change of metabolites in the glycolytic pathway, and consequential carbohydrates accumulation due to OsFBA1 disruption. Transcriptomics profiling corroborated the expression changes of photosynthesis, and carbon metabolism pathway genes. We further demonstrated that OsFBA1 serves as the primary FBA enzyme governing energy generation, photosynthesis and carbon metabolism. These results prove that OsFBA1 is an essential core gene in supporting the life cycle of rice, its expression has to be tightly regulated.