55| VOLUME 78 ISSUE 2 | NOVEMBER Open Access Characterization of intron 7 to exon 8 of heat shock protein 90-aa1 (hsp90aa1) gene in dominant brown layer chicken using some bioinformatic tools Young IRIVBOJE 1,2* , Adeboye FAFIOLU 1,3 , Oluwabusayo IRIVBOJE 1,4 and Christian IKEOBI 1,2 1 World Bank Centre of Excellence in Agricultural Development and Sustainable Environment, Federal University of Agriculture, Abeokuta, Nigeria 2 Department of Animal Breeding and Genetics, Federal University of Agriculture, P.M.B. 2240 Abeokuta, Nigeria 3 Department of Animal Nutrition, Federal University of Agriculture, P.M.B. 2240 Abeokuta, Nigeria 4 Agricultural Technology Department, The Federal Polytechnic, Ilaro, Nigeria * Corresponding author: Y. Irivboje e-mail: youngiriv@yahoo.com RESEARCH ARTICLE Abstract HSP90AA1, an isoform of HSP90 has been characterized to indicate it plays important roles in basic cellular events. It is activated in chicken in response to heat stress. This study was aimed at the computational analysis of the biochemical cum structural features and an evolutionary relationship study on the HSP90AA1 gene in Dominant brown layers (DBL) and some selected avian species using bioinformatics tools. ProtParam for physicochemical properties. Scanprosite for post-translational modification sites, Netphos-3.1 for phosphorylation sites, BDM-PUB program for Ubiquitination sites, PDBSUM for Secondary structure and homology modelling with SWISS-model. The findings revealed that intron 7 and exon 8 of HSP90AA1 protein in DBL had a molecular weight of 24681.19Da and an instability index of 27.60, contains N-myristoylation, Protein- kinase-C-phosphorylation and Tyrosine-kinase-phosphorylation site-2 post-translational modification sites, 4- serine and 2-threonine phosphorylation sites and 12-ubiquitination sites. The evolutionary relationship study found Japanese quail to be in a sister branch close to DBL and chicken. Motifs detected in the avian species revealed the gene to be highly conserved. The secondary structure consisted of 16-helices, 3-sheets and 14- strands. The homology modelling was 87.25% sequence identity with human MC-HSP90-alpha. The study elucidates the components and characteristics of HSP90AA1 in DBL in response to heat stress. Keywords: HSP90AA1; dominant brown layers; motifs; protein structure; phylogeny; phosphorylation. INTRODUCTION Heat shock proteins (HSPs) are primarily known for the protection of cells from the deleterious effect of stress (Timperio et al., 2008; Kalmar and Greensmith, 2009). The expression of most HSPs is increased if cells are exposed to elevated temperature or other stressful conditions, although some HSPs are expressed even in non-stressful conditions (Itoh et al., 2005). Through protein-protein interactions, HSPs also regulate fundamental cellular processes such as protein turnover, mitochondrial and endoplasmic reticulum trafficking, cell cycle progression, and steroid signalling (Beato and Klug, 2000; Taipale et al., 2010).Heat shock proteins are named according to their molecular weight, such as HSP60 for 60-kiloDalton, HSP70 for 70-kiloDalton, HSP90 for 90-kiloDalton, HSP100 for 100-kiloDalton, and so on (Schlesinger, 1990). The HSP90 which is commonly known to be ubiquitous and highly conserved protein is comprised up Received: 06 March 2021 Accepted: 04 October 2021 Published: 15 November 2021 DOI: 10.15835/buasvmcn-asb:2021.0005 © 2021 Authors. The papers published in this journal are licensed under the Creative Commons Attribution- NonCommercial-NoDerivatives 4.0 International License