Abstract
Acyl-coA binding proteins could transport acyl-coA esters from plastid to endoplasmic reticulum, prior to fatty acid biosynthesis, leading to the formation of triacylglycerol. The structure and the subcellular localization of acyl-coA binding proteins (ACBP) in Brassica napus were computationally predicted in this study. Earlier, the structure analysis of ACBPs was limited to the small ACBPs, the current study focused on all four classes of ACBPs. Physicochemical parameters including the size and the length, the intron-exon structure, the isoelectric point, the hydrophobicity, and the amino acid composition were studied. Furthermore, identification of conserved residues and conserved domains were carried out. Secondary structure and tertiary structure of ACBPs were also studied. Finally, subcellular localization of ACBPs was predicted. The findings indicated that the physicochemical parameters and subcellular localizations of ACBPs in Brassica napus were identical to Arabidopsis thaliana. Conserved domain analysis indicated that ACBPs contain two or three kelch domains that belong to different families. Identical residues in acyl-coA binding domains corresponded to eight amino acid residues in all ACBPs of B. napus. However, conserved residues of common ACBPs in all species of animal, plant, bacteria and fungi were only inclusive in small ACBPs. Alpha-helixes were displayed and conserved in all the acyl-coA binding domains, representing almost the half of the protein structure. The findings confirm high similarities in ACBPs between A. thaliana and B. napus, they might share the same functions but loss or gain might be possible.
Highlights
The function of proteins depends greatly on their structure
Analysis indicated that small BnACBPs contained 3 introns and 4 exons. 5 introns and 6 exons (BnaA02g10270D, BNnaA01g16660D, BnaC02g44810D) or 6 introns and 7 exons (BnaC01g20440D) were detected in ankyrin repeats BnACBPs. 2 introns and 3 exons (BnaA03g46540D, BnaC01g16110D, BnaC07g38820D) or 3 introns and 4 exons (BnaA01g13710D) were identified in large BnACBPs
MultiLoc2 showed that ankyrin repeats and large BnACBPs were mainly located in endoplasmic reticulum, while small and kelch BnACBPs were mainly located in the cytoplasm (S3 Table). These results suggested that small and kelch motif acyl-coA binding proteins (ACBP) were located in the cytoplasm and the ankyrin repeats and large ACBPs were secretory proteins that were located in endoplasmic reticulum
Summary
The function of proteins depends greatly on their structure. A small change or difference in their structure may alter the original function and may cause harmful effects. The acyl-coA binding proteins (ACBPs) are highly conserved across species and paralogues have evolved leading to multiple important functions [1]. ACBPs could transport fatty acid to endoplasmic reticulum after their biosynthesis into the plastid [2, 3, 4]. These fatty acids are involved in the biosynthesis of triacylglycerol (TAG), the most important compound of food or PLOS ONE | DOI:10.1371/journal.pone.0129650. These fatty acids are involved in the biosynthesis of triacylglycerol (TAG), the most important compound of food or PLOS ONE | DOI:10.1371/journal.pone.0129650 June 11, 2015
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