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Free keywords:
CO2-CONCENTRATING MECHANISM; FORM-I; ASSEMBLY CHAPERONE;
ATOMIC-RESOLUTION; PROTEIN; ACTIVASE; PHOTOSYNTHESIS; COLI;
IDENTIFICATION; MAINTENANCEBiochemistry & Molecular Biology;
Abstract:
A major challenge faced by human civilization is to ensure that agricultural productivity keeps pace with population growth and a changing climate. All food supply is generated, directly or indirectly, through the process of photosynthesis, with the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase ( Rubisco) catalyzing the assimilation of atmospheric CO2. Despite its pivotal role, Rubisco is a remarkably inefficient enzyme and must be made by plants in large quantities. However, efforts to enhance Rubisco performance by bioengineering have been hampered by its extensive reliance on molecular chaperones and auxiliary factors for biogenesis, metabolic repair, and packaging into membraneless microcompartments. Here, we review recent advances in understanding these complex machineries and discuss their implications for improving Rubisco carboxylase activity with the goal to increase crop yields.
