CHARACTERIZATION OF ATP GENE IN Calotropis procera MITOCHONDRIAL GENOME

Authors

  • S. E. HASSANEIN Bioinformatics and Computer Networks Department, Agricultural Genetic Engineering Research Institute (AGERI), Agriculture Research Center (ARC), Giza, Egypt College of Biotechnology, Misr University for Science and Technology (MUST), 6th October City, Egypt

Abstract

The drought-tolerant wild plant C. procera is important in medicine, industry and ornamental fields. Generally, its bark and leaves are used for many Folk medicine treatments. ATP4 (mitochondrion ATPase subunit 4), one of ATP gene family provides instructions for making transporter proteins called ATPases, which use energy from ATP molecule to move substances, such as fats, sugars, charged atoms or molecules (ions), and drugs, across the cell membranes. In this study, we uncovered and characterized ATP4 (ATP4, NCBI accession no. KP171515) gene in this medicinal plant from the de novo assembled transcriptome contigs of the high-throughput sequencing dataset. A number of GenBank accessions for ATP4 sequences were blasted with the recovered de novo assembled contigs. Homology modeling of the deduced amino acids was further carried out using Swiss-Model, accessible via the EXPASY. Superimposition of C. procera ATP4 full sequence model on Chain A, Subcomplex of the Stator of Bovine Mitochondrial ATP Synthase (PDB accession no. 2CLY_A) was constructed using RasMol and Deep-View programs. The functional domains of the novel ATP4 amino acids sequence were identified from the NCBI conserved domain data-base (CDD, accession no. cl21478) that provide insights into sequence structure/function relationships, as well as domain models imported from a number of external source databases (Pfam, SMART, COG, PRK, TIGRFAM).

References

S. M. Girgis and M. I. Hanna (2013). Identification and Expression of ATP Synthase F0 Subunit 6 in Tilapia Fish during Temperature Acclimation. Research Journal of Pharmaceutical, Biological and Chemical Sciences (RJPBCS), 4: 288-298.

Duke, J. A., Mary Jo Bogenschutz-Godwin, Judi duCellier and P. K. Duke (2002). Handbook of medicinal herbs. CRC PRESS, 2nd ed.

Haas, B. J., A. Papanicolaou, M. Yassour, M. Grabherr, P. D. Blood, J. Bowden, M. B. Couger, D. Eccles, B. Li, M. Lieber, M. D. Macmanes, M. Ott, J. Orvis, N. Pochet, F. Strozzi, N. Weeks, R. Westerman, T. William, C. N. Dewey, R. Henschel, R. D. Leduc, N. Friedman and A. Regev (2013). De novo transcript sequence reconstruction from RNA-seq using the Trinity platform for reference generation and analysis. Nat. Protoc., 8: 1494-512.

Krzywinski, M. I., J. E. Schein, I. Birol, J. Connors, R. Gascoyne, D. Horsman, S. J Jones and M. A M. Circos (2009). An information aesthetic for comparative genomics. Genome Res., 19: 1639-1645.

Kyte, J. and R. Doolittle (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157: 105132.

Nijtmans, L. G. J., N. S. Henderson, G. Attardi and I. J. Holt (2001). Impaired ATP Synthase Assembly Associated with a Mutation in the Human ATP Synthase Subunit 6 Gene. J. Biol. Chem., 276: 6755-6762.

Nijtmans, L. G., P. Klement, J. Houstek and C. van den Bogert (1995). F1-ATPase asubunit made up from two fragments is stabilized by ATP and complexes containing it obey altered kinetics. Biochim. Biophys. Acta, 1272: 190-198.

Pedersen, P. L. (2008). Transport ATPases into the year 2008: A brief overview related to types, structures, functions and roles in health and disease. J Bioenerg Biomembr, 39: 349-355.

Velours, J., G. A. de Chateaubodeau, M. Galante and B. Gukrin (1987). Subunit 4 of ATP synthase (F0F1) from yeast mitochondria; Purification, aminoacid composition and partial N-terminal sequence. Eur. J. Biochem., 164: 579-584.

Velours, J., P. Durrens, M. Aigle and B. Guerin (1988). ATP4, the structural gene for yeast FoFl ATPase subunit 4. Eur. J. Biochem., 170: 637-642.

Velours, J., M. Esparza, J. Hoppe, W. Sebald and B. Guerin (1984). Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae. EMBO J., 3: 207-212.

Ye Y. and A. Godzik (2003). Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics, 19: II246-II255.

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2016-01-12

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