Abstract
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is considered to be a housekeeping glycolytic enzyme that catalyzes an important energy-yielding step in carbohydrate metabolism in the cytoplasm. However, GAPDH participates in several other biological activities via the changes of its subcellular localization, which depends largely on the modifications of its catalytic active site Cys residue. In this study, we demonstrated that the active site mutation C154S induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present mainly in the cytoplasm. However, the C-terminal truncated mutant of GAPC, GAPC△C-GFP was present mainly in nuclei in rice protoplast. The further interaction analysis indicated that the GAPC△C disrupted the dimeric GAPC formation, may thus, facilitating its nuclear localization. The result suggested that the nuclear translocation of GAPDH also depends on its oligomeric forms in rice.
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