COMPREHENSIVE SCREENING OF NITRILE-SPECIFIER PROTEINS IN BRASSICACEAE FAMILY: AN In Silico STUDY

Abstract

Clucosinolates (GLs) are beta-thioglucoside N-hydroxysulfates found in the angiosperm plant families, mainly present in the order Brassicales. The myrosinase enzyme catalyzes the hydrolysis of the thioglucosidic bond in the GL structure, consequently, an unstable aglucone moiety is released. Spontaneous rearrangement of the aglucone yields isothiocyanates that are toxic to many organisms. Brass icaceae species have specifier proteins that promote aglucone to form different groups of substances such as simple nitriles, epithionitriles and organic thiocyanates. The generation of epithionitriles and organic thiocyanates requires the presence of epithiospecifier protein (ESP) and thiocyanate-forming protein (TFP), respectively. Nitrile-specifier proteins (NSPs) promote the simple nitrile formation. The aim of this work was to make a detailed bioinformatics analysis of NSPs found in the family of Brass icaceae. NSP open reading frames (ORF) in Brass icaceae genomes were scanned in silico. Thus, we created a dataset containing 57 predicted NSPs from different species of Brassicaceae family. Computational analysis revealed that Brassicaceae NSPs were acidic and stability and sobbility were high. It has been seen that NSPs may found in different chromosomes in varying numbers in the genome. Finally, phylogenetic analysis of Brass icaceae NSPs showed similarities with the major lineages reported in previous phybgenetic studies of Brassicaceae.