Fig. 4: (a) Molecular structure of CpATFL1. The protein
structure was built based on the ab initio approach from the
QUARK server. The highlighted pink region represents the conserved
critical amino acids for the activity of TFL1 as a repressor with a
reference amino acid, Phe at the position 120, situated towards the
bottom region. (b) Multiple sequence alignment of FT and TFL1
homologues in A. thaliana (ATH), Zea mays (ZCN), O.
sativa (Os), B. distachyon and C. pallens. Sequences
were aligned using the MUSCLE alignment tool. The level of conservation
of amino acids is represented by the colour graph at the bottom of the
alignment. Red represents stronger conservation while black represents
variable amino acid sites. The red asterisk represents the critical
amino acid change (Glu-> Gln) in CpATFL1 which may be
responsible for its floral-promoting activity. (c) Codon usage
between ZCN1, a TFL1 homologue in Z. mays, and CpATFL1. *
represents the single nucleotide change coding for amino acid at
position 150. (d) Electrostatic surface charge for ZCN8, ZCN1
and CpATFL1 . Electrostatic surface potential for each sequence was
calculated from the CHARMM server. Protein structures were viewed using
the pymol represented by the amino acid at position 150 and a reference
amino acid, Phe, at position 120 to orient the structures.