INTRODUCING THE CEREAL THYLAKOID FK506-BINDING PROTEINS: LITTLE ENZYMES WITH A BRIGHT FUTURE

摘要

The FK506- and rapamycin-binding proteins (FKBPs) were first discovered as the cellular receptor proteins for the immunosuppressant compounds FK506 and rapamycin (Harding et al., 1989). Since then, the FKBPs have been identified in all organisms studied, often comprising large protein families, and their cellular roles have been extended to include peptidyl prolyl cis/trans isomerase (PPIase) and molecular chaperone activity. The FKBP family of higher plants consists of over twenty members and half of these are residents of the chloroplast thylakoid, contributing significantly to the thylakoid proteome and conceivably exerting some influence on plant photosynthesis. Considering the crucial nature of photosynthesis to the manufacture of plant carbohydrates, an exploration of functionality for the lumenal FKBPs in cereals appears warranted. This work presents an analysis of the genes encoding the thylakoid lumen-localised FKBPs in wheat, rice and sorghum.