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      Computational genome-wide identification of heat shock protein genes in the bovine genome

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          Abstract

          Background: Heat shock proteins (HSPs) are molecular chaperones known to bind and sequester client proteins under stress.

          Methods: To identify and better understand some of these proteins, we carried out a computational genome-wide survey of the bovine genome. For this, HSP sequences from each subfamily (sHSP, HSP40, HSP70 and HSP90) were used to search the Pfam (Protein family) database, for identifying exact HSP domain sequences based on the hidden Markov model. ProtParam tool was used to compute potential physico-chemical parameters detectable from a protein sequence. Evolutionary trace (ET) method was used to extract evolutionarily functional residues of a homologous protein family.

          Results: We computationally identified 67 genes made up of 10, 43, 10 and 4 genes belonging to small HSP, HSP40, HSP70 and HSP90 families respectively. These genes were widely dispersed across the bovine genome, except in chromosomes 24, 26 and 27, which lack bovine HSP genes. We found an uncharacterized outer dense fiber ( ODF1) gene in cattle with an intact alpha crystallin domain, like other small HSPs. Physico-chemical characteristic of aliphatic index was higher in HSP70 and HSP90 gene families, compared to small HSP and HSP40. Grand average hydropathy showed that small HSP (sHSP), HSP40, HSP70 and HSP90 genes had negative values except for DNAJC22, a member of HSP40 gene family. The uniqueness of DNAJA3 and DNAJB13 among HSP40 members, based on multiple sequence alignment, evolutionary trace analysis and sequence identity dendrograms, suggests evolutionary distinct structural and functional features, with unique roles in substrate recognition and chaperone functions. The monophyletic pattern of the sequence identity dendrograms of cattle, human and mouse HSP sequences suggests functional similarities.

          Conclusions: Our computational results demonstrate the first-pass in-silico identification of heat shock proteins and calls for further investigation to better understand their functional roles and mechanisms in Bovidae.

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          Most cited references45

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          ExPASy: The proteomics server for in-depth protein knowledge and analysis.

          The ExPASy (the Expert Protein Analysis System) World Wide Web server (http://www.expasy.org), is provided as a service to the life science community by a multidisciplinary team at the Swiss Institute of Bioinformatics (SIB). It provides access to a variety of databases and analytical tools dedicated to proteins and proteomics. ExPASy databases include SWISS-PROT and TrEMBL, SWISS-2DPAGE, PROSITE, ENZYME and the SWISS-MODEL repository. Analysis tools are available for specific tasks relevant to proteomics, similarity searches, pattern and profile searches, post-translational modification prediction, topology prediction, primary, secondary and tertiary structure analysis and sequence alignment. These databases and tools are tightly interlinked: a special emphasis is placed on integration of database entries with related resources developed at the SIB and elsewhere, and the proteomics tools have been designed to read the annotations in SWISS-PROT in order to enhance their predictions. ExPASy started to operate in 1993, as the first WWW server in the field of life sciences. In addition to the main site in Switzerland, seven mirror sites in different continents currently serve the user community.
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            An evolutionary trace method defines binding surfaces common to protein families.

            X-ray or NMR structures of proteins are often derived without their ligands, and even when the structure of a full complex is available, the area of contact that is functionally and energetically significant may be a specialized subset of the geometric interface deduced from the spatial proximity between ligands. Thus, even after a structure is solved, it remains a major theoretical and experimental goal to localize protein functional interfaces and understand the role of their constituent residues. The evolutionary trace method is a systematic, transparent and novel predictive technique that identifies active sites and functional interfaces in proteins with known structure. It is based on the extraction of functionally important residues from sequence conservation patterns in homologous proteins, and on their mapping onto the protein surface to generate clusters identifying functional interfaces. The SH2 and SH3 modular signaling domains and the DNA binding domain of the nuclear hormone receptors provide tests for the accuracy and validity of our method. In each case, the evolutionary trace delineates the functional epitope and identifies residues critical to binding specificity. Based on mutational evolutionary analysis and on the structural homology of protein families, this simple and versatile approach should help focus site-directed mutagenesis studies of structure-function relationships in macromolecules, as well as studies of specificity in molecular recognition. More generally, it provides an evolutionary perspective for judging the functional or structural role of each residue in protein structure.
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              Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance.

              Cells from virtually all organisms respond to a variety of stresses by the rapid synthesis of a highly conserved set of polypeptides termed heat shock proteins (HSPs). The precise functions of HSPs are unknown, but there is considerable evidence that these stress proteins are essential for survival at both normal and elevated temperatures. HSPs also appear to play a critical role in the development of thermotolerance and protection from cellular damage associated with stresses such as ischemia, cytokines, and energy depletion. These observations suggest that HSPs play an important role in both normal cellular homeostasis and the stress response. This mini-review examines recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging.
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                Author and article information

                Contributors
                Role: Data CurationRole: Formal AnalysisRole: InvestigationRole: Writing – Original Draft Preparation
                Role: Formal AnalysisRole: ValidationRole: Writing – Review & Editing
                Role: ConceptualizationRole: Formal AnalysisRole: SoftwareRole: ValidationRole: VisualizationRole: Writing – Review & Editing
                Role: Data CurationRole: InvestigationRole: Methodology
                Role: Funding AcquisitionRole: InvestigationRole: Supervision
                Role: Data CurationRole: Formal AnalysisRole: InvestigationRole: Methodology
                Role: Formal AnalysisRole: MethodologyRole: SupervisionRole: Writing – Review & Editing
                Role: InvestigationRole: Methodology
                Role: ConceptualizationRole: Funding AcquisitionRole: InvestigationRole: Project AdministrationRole: ResourcesRole: SupervisionRole: ValidationRole: VisualizationRole: Writing – Review & Editing
                Journal
                F1000Res
                F1000Res
                F1000Research
                F1000Research
                F1000 Research Limited (London, UK )
                2046-1402
                20 September 2018
                2018
                : 7
                : 1504
                Affiliations
                [1 ]Department of Animal Breeding and Genetics, Federal University of Agriculture, Abeokuta, Nigeria
                [2 ]International Programs, College of Agriculture and Life Sciences, Cornell University, Ithaca, NY, 14853, USA
                [3 ]Department of Animal Science, Berry College, Mount Berry, GA, 30149, USA
                [4 ]Departamento Regional de Bioingenierias, Tecnologico de Monterrey, Escuela de Ingenieria y Ciencias, Queretaro, Mexico
                [5 ]Department of Animal Production and Health, Federal University of Agriculture, Abeokuta, Nigeria
                [6 ]Usomi Limited, Nairobi, Kenya
                [7 ]Department of Animal Production and Health, Federal University of Technology, Akure, Nigeria
                [8 ]Department of Biomedical Sciences, Rochester Institute of Technology, Rochester, NY, 14623, USA
                [9 ]School of Life Sciences, University of KwaZulu-Natal, Durban, 4000, South Africa
                [10 ]School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30032, USA
                [11 ]African Institute of Bioscience Research and Training, Ibadan, Nigeria
                [1 ]Indian Institute of Toxicology Research (CSIR-IITR), (CSIR - Council of Scientific & Industrial Research) , Lucknow,  Uttar Pradesh, India
                [1 ]Bio Nano Electronics Research Centre, Graduate School of Interdisciplinary Science, Toyo University, Kawagoe, Japan
                [2 ]Department of Pharmaceutical Science, Jefferson College of Pharmacy, Thomas Jefferson University, Philadelphia, PA, USA
                [1 ]Grupo de Biología y Toxicología Ambiental, Departamento de Física Matemática y de Fluidos, Universidad Nacional de Educación a Distancia, UNED, Madrid, Spain
                Author notes

                No competing interests were disclosed.

                Competing interests: No competing interests were disclosed.

                Competing interests: No competing interests were disclosed.

                Competing interests: No competing interests were disclosed.

                Author information
                https://orcid.org/0000-0002-9758-8116
                https://orcid.org/0000-0002-3271-8442
                Article
                10.12688/f1000research.16058.1
                6259560
                30542619
                791fb2d9-2b12-4c00-82e2-d9f6d7061139
                Copyright: © 2018 Ajayi OO et al.

                This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 12 September 2018
                Funding
                Funded by: Cornell University Agricultural Experiment Station
                Funded by: National Institute of Food and Agriculture
                Award ID: 2010-34444-20729
                Award ID: 2006-35205-16864
                Award ID: 2009-65205-05635
                Funded by: Zoetis
                Funded by: United States Agency for International Development
                Funded by: U.S. Department of Agriculture
                We are thankful for financial support by the College of Agriculture and Life Sciences, Cornell University, Ithaca, NY and Zoetis, Inc. Additional support by National Research Initiative Competitive Grant Program (Grant No. 2006-35205-16864) from the USDA National Institute of Food and Agriculture; USDA-NIFA Research Agreements (Nos. 2009-65205-05635, 2010-34444-20729) and USDA Federal formula Hatch funds appropriated to the Cornell University Agricultural Experiment Station are gratefully acknowledged. OOA was supported by a Norman Borlaug Leadership Enhancement in Agriculture Program fellowship from the US Agency for International Development.
                The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Research Article
                Articles

                cattle,bovine genome,heat shock proteins,hsp genes,molecular chaperones

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