Putative fructose-1,6-bisphosphate aldolase 1 (AtFBA1) affects stress tolerance in yeast and Arabidopsis

• Published in: Journal of Plant Biotechnology Vol. 39; no. 2; pp. 106 - 113
• Main Authors: Moon, S.J., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Shin, D.J., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Kim, B.G., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Byun, M.O., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea
• Format: Journal Article
• Language: English
• Published: 한국식물생명공학회 01.06.2012
• Subjects: ARABIDOPSIS; Germination assay; NaCl; 농학
• ISSN: 1598-6365; 1229-2818; 2384-1397
• DOI: 10.5010/JPB.2012.39.2.106

Glycolysis is responsible for the conversion of glucose into pyruvate and for supplying reducing power and several metabolites. Fructose-1,6-bisphosphate aldolase (AtFBA1), a central enzyme in the glycolysis pathway, was isolated by functional complementation of the salt-sensitive phenotype of a calcineurin (CaN)-deficient yeast mutant. Under high salinity conditions, aldolase activity and the concentration of NADH were compromised. However, expression of AtFBA1 maintained aldolase activity and the NADH level in yeast cells. AtFBA1 shares a high degree of sequence identity with known class I type aldolases, and its expression was negatively regulated by stress conditions including NaCl. The fusion protein GFP-AtFBA1 was localized in the cytosol of Arabidopsis protoplasts. The seed germination and root elongation of AtFBA1 knock-out plants exhibited sensitivity to ABA and salt stress. These results indicate that AtFBA1 expression and aldolase activity is important for stress tolerance in yeast and plants.