Molecular cloning, bioinformatics analysis, and expression of small heat shock protein beta-1 from Camelus dromedarius, Arabian camel
| Autor: | Sultan N. Alharbi, Abdulmalek T. Algarni, Manee M. Manee, Basel M. Alnafjan, Mohammad N. Alkhrayef, Waleed M. Alghamdi, Musaad A. Altammami |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular Protein Structure Comparison 0301 basic medicine Untranslated region Gene Expression lcsh:Medicine Protein Structure Prediction Biochemistry Protein Structure Secondary Heat Shock Response Database and Informatics Methods Protein structure Camels Macromolecular Structure Analysis Cloning Molecular lcsh:Science Peptide sequence Heat-Shock Proteins Phylogeny Cellular Stress Responses Mammals Multidisciplinary Eukaryota Cell Processes Vertebrates Sequence Analysis Research Article Protein Structure Multiple Alignment Calculation endocrine system Camelus DNA Complementary Bioinformatics Sequence alignment Biology Molecular cloning Real-Time Polymerase Chain Reaction Research and Analysis Methods 03 medical and health sciences Complementary DNA Computational Techniques Genetics Animals Bactrian camel Amino Acid Sequence RNA Messenger Molecular Biology Sequence Homology Amino Acid 030102 biochemistry & molecular biology lcsh:R Organisms Computational Biology Biology and Life Sciences Proteins Cell Biology biology.organism_classification Molecular biology Split-Decomposition Method eye diseases Open reading frame 030104 developmental biology Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Amniotes lcsh:Q 5' Untranslated Regions Sequence Alignment Chromatography Liquid |
| Zdroj: | PLoS ONE, Vol 12, Iss 12, p e0189905 (2017) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | Small heat shock protein beta-1 (HSPB-1) 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 HSPB-1 gene is available for many mammalian species, the HSPB-1 gene of Arabian camel (Arabian camel HSPB-1) has not yet been structurally characterized. We cloned and functionally characterized a full-length of Arabian camel HSPB-1 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 HSPB-1 mRNA was examined using quantitative real-time PCR (qRT-PCR); which suggested that Arabian camel HSPB-1 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 HSPB-1 protein confirmed the identity of this protein. Phylogenetic analysis showed that the HSPB-1 protein of Arabian camel is grouped together with those of Bactrian camel and Alpaca. Comparing the modelled 3D structure of Arabian camel HSPB-1 protein with the available protein 3D structure of HSPB-1 from human confirmed the presence of α-crystallin domain, and high similarities were noted between the two structures by using super secondary structure prediction. |
| Databáze: | OpenAIRE |
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