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- Title
Structural study of the Annexin evolution in Fungi.
- Authors
Gharehbolagh, Sanaz Aghaei; Dasmeh, Pouria; Sadeghi, Solmaz; Marashiyan, Mahya; Rahimi, Hamzeh
- Abstract
Introduction: The annexins are a large family of proteins that bind to Ca2+ and cell membrane phospholipids. These proteins are composed of two domains: N-terminal domain that interacts with membrane phospholipids and C-terminal domains that interacts with other annexins and proteins. Annexins implicated in variety functions such as exocytosis and endocytosis, signal transduction, organization of the extracellular matrix, resistance to reactive oxygen species, subcellular transport, membrane repair, and DNA replication. Moreover it has been suggested that they have a critical role on the tip growth of fungal hypha. The aim of this study is using bioinformatics methods to study of sequence diversity and structural evolution of fungal annexins. Materials and Methods: In this study, amino acid sequence of fungal annexins was retrieved from NCBI and UNIPROT databases. Then multiple sequence alignment and phylogentic investigated by Clustal and Omega software. The positive selection performed by means of Data monkey web server. Then protein structure prediction and molecular dynamic were performed using MODELLER9v12 and Gromacs, respectively. Result: The obtained results of the study on 48 fungal annexins showed these proteins in fungi have four repeats in Cterminal domain that each repeat composed of approximately 60 amino acids. Results of selection mapped on the phylogenetic tree showed strength of selection in some fungi such as Paracoccidioides and Emericella that are pathogen in human or Ustilago maydis that causes smut on maize and teosinte was high. Conclusion: The results indicated fungal annexin can be correlated with pathogenicity of some fungal pathogens.
- Subjects
IRAN; CALCIUM-binding proteins; CONFERENCES &; conventions; BIOLOGICAL evolution; FUNGI; BIOINFORMATICS
- Publication
Current Medical Mycology, 2018, Vol 4, p149
- ISSN
2423-3439
- Publication type
Article
- DOI
10.18502/cmm.4.S1.2018.180