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Molecular Plant Breeding 2011, Vol.2, No.16, 109
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arginine and the 81
st
tyrosine were considered as the
key sites where LTP functions with lipid molecules in
vitro conditions (Han et al., 2001), indicating that the
two sites had highly conservative in the sequence.
Figure 3 Alignment analysis of amino acid sequences of cloned SCAs compared with LTP in in families of liliaceous and gramineous
plants
Note: “*” show the same amino acid. Eight conserved cysteine amino acid residues are shown as boldface asterisks (
*
). Two
consensus pentapeptide motifs are shown in boxes. The key sites highlighted with grey color which interact with lipid molecules of
maize LTP. The differences among the species of amino acid residues were highlighted by yellow and purple. The figures of the left
four columns represent gene homology. Sequence data are adopted from maize LTP (Acc. No. AAA33493), rice LTP (Acc. No.
AAB70541),
Lilium longiflorum
SCA (Acc. No. Q9SW93) and
Lilium formosanum
LfLTP (Acc. No. ACP30545)
1.4 Phylogenetic tree construction and secondary
structure prediction of SCA
Ten amino acid sequence of Lily SCA except LaSCA2
and fifty seven known amino acid sequences of other
plant LTP were employed to do alignment analysis to
build the phylogenetic tree (Figure 4). It was found
that the cloned ten sequences were clustered into a
group with
Lilium longiflorum
'Nellie white' SCA and
the Taiwan lily LfLTP together, indicating that their
evolutionary relationship should be the closest. The
different SCA copies from the same variety can be
well clustered together, Asian lily SCA and Taiwan
lily LfLTP went into a group, while Easter lily 'White
heaven' SCA and Easter lily 'Nellie white' SCA came
to a group. The dendrogram also presented that the
genetic distance between Asian Lily and Easter lily