Effect of Amino Acid Point Mutations on the Structure and Func-tion of Phytochrome B in Arabidopsis thaliana
Organisms have evolved different photoreceptors to adapt to the ever-changing conditions of the external light environment.Phytochromes(phys)are one of the classic plant photoreceptors,mainly perceiving red and far-red light.Phytochromes detect red and far-red light through the light conversion between the dark-adapted Pr state and the light-activated Pfr state.All plant phytochromes have a conserved N-terminal photoreceptor region and a C-terminal regulatory region.The N-terminal includes NTE,PAS,GAF,and PHY subdomains,while C-terminal includes two PAS domains and a histidine kinase-related domain(HKRD).In order to understand how the structure of photochromes con-trols its function,many function-deficient photochrome derivatives and amino acid point mutants have been obtained and studied.The N-terminal domain plays important roles in the spectral properties,light signal perception and light signal transduction of phyB.The C-terminal domain is essential for dimerization and nuclear localization of photochrome.This paper mainly reviews point mutations of amino acid in various subdomains of phyB in Arabidopsis thaliana and their ef-fects on the function of phyB,in order to have a better understanding of the structure and functional regulation of phyB.It lays a foundation for obtaining crops with desired agronomic characteristics through gene editing.
phyBArabidopsis thalianadomainamino acid point mutationfunction
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