Jm. Bradley et al., IDENTIFICATION OF PHYTOCHROME-B AMINO-ACID-RESIDUES MUTATED IN 3 NEW PHYB MUTANTS OF ARABIDOPSIS-THALIANA, Journal of Experimental Botany, 47(302), 1996, pp. 1449-1455
The growth and development of plants is regulated by light via the act
ion of photoreceptors which are responsive to the red/far-red, blue an
d UV regions of the spectrum. Phytochrome B (the apoprotein of which i
s encoded by the PHYB gene) is one of the red/far-red absorbing photor
eceptors active in this process, In this paper, the isolation and char
acterization of three new EMS-induced mutations of Arabidopsis which c
onfer phytochrome B deficiency are described. Complementation analysis
showed that these mutations (phyB-101, phyB-102 and phyB-104) were al
lelic with PHYB, DNA sequence analysis showed that all three mutants c
ontain nucleotide substitutions in the PHYB gene sequence. phyB-101 ca
rries a nucleotide substitution within the second exon of the PHYB gen
e. This G-to-A substitution is a missense mutation that converts a glu
tamate residue at position 812 of the phytochrome B apoprotein to a ly
sine residue, phyB-102, another missense mutant, carries a C-to-T subs
titution which converts a serine residue at position 349 of the phytoc
hrome B apoprotein to a phenylalanine residue. phyB-104 carries a prem
ature stop codon as a result of a G-to-A mutation 1190 bp down-stream
of the ATG start codon of the PHYB sequence, The missense mutations in
phyB-101 and phyB-102 cause significant alterations in the predicted
secondary structure of their respective mutant polypeptides, and ident
ify amino acid residues playing crucial roles in phytochrome B functio
n, assembly or stability.