Page 713 - e-Book

B

C

D

E

Figure 1: Variations observed in the low complexity regions (pink) and transmembrane
regions (blue) (a) Hordeum vulgare had only nine transmembrane regions but no N-ternimal

low complexity region (b) Oryza sativa depicted only one low complexity region (c)

Arabidopsis thaliana had three low complexity regions (d) the reference Jatropha curcas
depicted one low complexity region and (E) the most variable Morus notabilis lacking the

last two transmembrane regions.
The smart domain analysis revealed that all the DGAT1 amino acid sequences studied in the

analysis showed highly conserved DGAT1 domain, particularly consisting of nine
transmembrane domains except for Morus notabilis lacking the last two transmembrane

domains. Most of the variations were observed in the N-teminal region consisting of low

complexity regions and signal peptides. The smallest protein sequences lack low complexity
regions (none in Hordeum vulgare, Figure 1 (a) and most of the DGAT1 proteins under

consideration contain one low complexity region (Oryza sativa, Jatropha curcas, Figure. 1

(b) and Figure. 1 (d) respectively) while three low complexity regions were observed in
Arabidopsis thaliana (also in Coffea caneophora). All the species were predicted to contain

low complexity regions towards the N-terminal region except for Helianthus annus, Echium
pitardii and Xanthoceras sorbifolium which contains a single low complexity region between

the transmembrane regions 4 and 5. There has not been any experimental evidence for effect
of this type of variation on the functioning of DGAT1 proteins. Interestingly, the most variant

Morus notabilis protein shows the absence of low complexity region along with two

transmembrane regions. Plant DGAT1 proteins are spanned with some functionally critical

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