Arabian camel <i>HSPB-1</i> mRNA expression levels in SACAS cells at control(37°C) and heat-stressed condition (42°C) for different time points.

<p>The results are expressed relative to that of <i>β</i>-actin as an endogenous control.</p

Molecular cloning, bioinformatics analysis, and expression of small heat shock protein beta-1 from <i>Camelus dromedarius</i>, Arabian camel

<div><p>Small heat shock protein beta-1 (<i>HSPB-1</i>) plays an essential role in the protection of cells against environmental stress.Elucidation of its molecular, structural, and biological characteristics in a naturally wild-type model is essential. Although the sequence information of the <i>HSPB-1</i> gene is available for many mammalian species, the <i>HSPB-1</i> gene of Arabian camel (Arabian camel <i>HSPB-1</i>) has not yet been structurally characterized. We cloned and functionally characterized a full-length of Arabian camel <i>HSPB-1</i> cDNA. It is 791 bp long, with a 5′-untranslated region (UTR) of 34 bp, a 3′-UTR of 151 bp with a poly(A) tail, and an open reading frame (ORF) of 606 bp encoding a protein of 201 amino acids (accession number: MF278354). The tissue-specific expression analysis of Arabian camel <i>HSPB-1</i> mRNA was examined using quantitative real-time PCR (qRT-PCR); which suggested that Arabian camel <i>HSPB-1</i> mRNA was constitutionally expressed in all examined tissues of Arabian camel, with the predominately level in the esophagus tissue. Peptide mass fingerprint-mass spectrometry (PMF-MS) analysis of the purified Arabian camel <i>HSPB-1</i> protein confirmed the identity of this protein. Phylogenetic analysis showed that the <i>HSPB-1</i> protein of Arabian camel is grouped together with those of Bactrian camel and Alpaca. Comparing the modelled 3D structure of Arabian camel <i>HSPB-1</i> protein with the available protein 3D structure of <i>HSPB-1</i> from human confirmed the presence of <i>α</i>-crystallin domain, and high similarities were noted between the two structures by using super secondary structure prediction.</p></div

Parker hydrophilicity prediction of Arabian camel <i>HSPB-1</i> protein.

<p>The threshold is 1.0. The regions having <i>β</i>-turns in the protein are shown in yellow color, above the threshold value.</p

Nucleotide and amino acid sequences of Arabian camel <i>HSPB-1</i> cDNA (GenBank accession no., MF278354).

<p>The numbers above the nucleotide sequence show the nucleotide positions. The stop codon is represented with an asterisk(*). The putative polyadenylation signal is shown in red.</p

The phylogenetic tree shows the relationship of camel <i>HSPB-1</i> protein and protein sequences from other species.

<p>Maximum likelihood tree based on complete coding sequences. Values at nodes are bootstrapping ≥ 49% obtained from 1000 resampling of the data.</p

Glob Plot analysis.

<p>Blue boxes are disordered regions, and green boxes are ordered regions in the Arabian camel <i>HSPB-1</i> protein.</p

Calculated and observed ions of peptide masses of Arabian camel <i>HSPB-1</i> protein.

<p>Calculated and observed ions of peptide masses of Arabian camel <i>HSPB-1</i> protein.</p

Chou and Fasman <i>β</i>-turns prediction of Arabian camel <i>HSPB-1</i> protein.

<p>The threshold is 1.00. The regions having <i>β</i>-turns in the protein are shown in yellow color.</p

Phylogenetic tree shows the classification of Arabian camel <i>HSPB-1</i> within the sHSPB family.

<p>Phylogenetic tree shows the classification of Arabian camel <i>HSPB-1</i> within the sHSPB family.</p

Karplus and Schulz flexibility prediction of Arabian camel HSPB-1 protein.

<p>The x-axis and y-axis represent the position and score, respectively. The threshold is 1.0. The flexible regions of the protein are shown in yellow color, above the threshold value.</p