Arabidopsis Homologues to the LRAT a Possible Substrate for New Plant-Based Anti-Cancer Drug Development

Arabidopsis Homologues to the LRAT a Possible Substrate for New Plant-Based Anti-Cancer Drug Development

Dimitrios Kaloudas (Sofia University “St. Kliment Ohridski”, Sofia, Bulgaria) and Robert Penchovsky (Sofia University “St. Kliment Ohridski”, Sofia, Bulgaria)
Copyright: © 2018 |Pages: 13
DOI: 10.4018/IJBCE.2018010103
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Abstract

This article describes how an NC gene family has been identified in the genome of the Arabidopsis thaliana (Arabidopsis) by homology to the human Lecithin Retinal Acyl Transferase (LRAT) and the picornavirus 2A protein. The Arabidopsis proteins contain two motifs identified in a vast variety of organisms, an H-Box and an NC. Among related proteins are the C. elegans EGL-26, a regulator protein of cell morphogenesis in the vulva region, and human proteins that might be related to cell proliferation or development. Human homologues include HRAS-like tumour suppressors, the Tazarotene-induced gene 3 (TIG3), and a deSumoylating Isopeptidase (PNAS-4) that induces apoptosis in lung cancer cells. Preservation of the two motifs observed in the Arabidopsis proteins in homology to tumour suppressors, and the conservation of residues important for the function of the LRAT amongst the Arabidopsis homologues can be indicative not only of the importance of these domains for the function of the plant proteins but can also reveal a new candidate group for the design of plant-based tumour-targeting drug development.
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Introduction

The H-Box/NC proteins were subsequently suggested to belong to a larger group of proteins, termed the NIpC/P60 superfamily. The NIpC/P60 superfamily was divided into four families according to their amino acid sequence similarities and motifs. The P60-like family, the ACMB/LytN-like divergent family, the lecithin retinal acyl transferase-like (LRAT-like) family and the YaeF/poxvirus G6R type family (Anantharaman & Aravind, 2003). The NIpC/P60 proteins are predicted to have a thiol-protease fold. This is made up of a β-strand region containing a conserved histidine, an orientating polar residue (part of a conserved GD [glucine-aspartic acid] motif) and a α-helix domain containing a conserved cysteine. Some members of the NIpC/P60 superfamily proteins (including the LRAT-like ones) exhibit circular permutation. In the thiol-protease fold area, variable sized inserts are often seen in the region between the strand containing the histidine and the strand bearing the orienting polar residue (Anantharaman & Aravind, 2003).

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