Table S1: Primer Sequences Used for Genomic PCR Amplification

Table S1: Primer sequences used for genomic PCR amplification

PRIMER NAME / SEQUENCE
UCP1F / 5’ ATGGTAGCTGATAGCAAATCCGA 3’
UCPF2 / 5’ AGTTAGACTTCAGGCCGAAGGGA 3’
UCP1R / 5’ TCAGTGTTTCTTGGACGAATCTA 3’
UCPR2 / 5’ TGCTTCACTTGATCGTAACTCGCT 3’

SUPPLEMENTARYFIGURE LEGENDS

Fig.S1: Illustrations highlighting the conserved domains of BjUCP1 protein determined using NCBI conserved domain database (

Fig. S2: Multiple sequence alignment of UCP1 from various plant species. Residues that are in red are conserved. Dotted black box shows the ETPS conserved motif in UCP1s. Double black underline highlights the UCP signatures. Solid purple underline depicts conserved Motif 1, while solid pink underline shows Motif 2. Motif 5 and Motif 6 specific to plant species are highlighted in blue and green box respectively. The figure was generated with Clustal Omega (Sievers et al. 2011) and ESPript (Robert and Gouet 2014).

Fig. S3:Predicted secondary structure by SOPMA using deduced amino sequence of BjUCP1 from B. juncea. Helices, sheets, turns and coils are indicated by the longest, second longest, second shortest and shortest vertical lines, respectively.

Fig. S4: Neighbor - Joining Phylogenetic tree constructed by MEGA 6.06 beta program using deduced amino sequence of BjUCP1 and protein sequences of UCP1 from other organisms. Numbers above indicate bootstrap values.Red box highlights the UCP1 sequences of Brassica genus while the green box highlights the UCP from animals (Human and house mouse).

Fig. S5: Three - dimensional models for BjUCP1. A B) Superimposition of 3 - D cartoon model of BjUCP1 (green) with known mitochondrial ADP/ATP carrier protein from Bos taurus i.e. cow (1OKCA, Blue) and mitochondrial uncoupling protein 2 from Mus musculus i.e. house mouse (2LCKA, firebrick red) respectively. The figures were generated with PyMOL.

Fig.S6: Visualization of transmembrane domains in BjUCP1. A) Secondary structure of BjUCP1 with residues highlighted in yellow are located in the transmembrane regions of the protein was predicted by MINNOU server ( Alpha helices, beta strand, random coil are indicated in red, green and blue respectively. B) Graphical representation of the predicted topology of BjUCP1 containing six transmembrane helices depicted as red rectangles by OCTOPUS program (

Fig.S7: Three- dimensional models for BjUCP1. AB) Ligand binding site of BjUCP1 as predicted by I-TASSER Web Server. B) The area shows the ball stick structure of the main amino acid residues which interact with ligand CXT.Main residues (pink) which participate in binding with ligand carboxyatractyloside (green-red-yellow sphere; CXT) are Arg84, Arg92, Tyr96, Gly125, Ile129, Arg185, Asn186, Ile189, Asn190, Gly232, Val235, Asp236 and Lys239. The figures were generated using PyMOL.