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Computational identification and phylogenetic analysis of the oil-body structural proteins, oleosin and caleosin, in castor bean and flax.
Gene. 2013 Feb 25; 515(2):454-60.GENE

Abstract

Oil bodies (OBs) are the intracellular particles derived from oilseeds. These OBs store lipids as a carbon resource, and have been exploited for a variety of industrial applications including biofuels. Oleosin and caleosin are the common OB structural proteins which are enabling biotechnological enhancement of oil content and OB-based pharmaceutical formations via stabilizing OBs. Although the draft whole genome sequence information for Ricinus communis L. (castor bean) and Linum usitatissimum L. (flax), important oil seed plants, is available in public database, OB-structural proteins in these plants are poorly indentified. Therefore, in this study, we performed a comprehensive bioinformatic analysis including analysis of the genome sequence, conserved domains and phylogenetic relationships to identify OB structural proteins in castor bean and flax genomes. Using comprehensive analysis, we have identified 6 and 15 OB-structural proteins from castor bean and flax, respectively. A complete overview of this gene family in castor bean and flax is presented, including the gene structures, phylogeny and conserved motifs, resulting in the presence of central hydrophobic regions with proline knot motif, providing an evolutionary proof that this central hydrophobic region had evolved from duplications in the primitive eukaryotes. In addition, expression analysis of L-oleosin and caleosin genes using quantitative real-time PCR demonstrated that seed contained their maximum expression, except that RcCLO-1 expressed maximum in cotyledon. Thus, our comparative genomics analysis of oleosin and caleosin genes and their putatively encoded proteins in two non-model plant species provides insights into the prospective usage of gene resources for improving OB-stability.

Authors+Show Affiliations

Department of Biochemistry, Division of Applied Life Science, Gyeongsang National University, Jinju 660-701, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

23232356

Citation

Hyun, Tae Kyung, et al. "Computational Identification and Phylogenetic Analysis of the Oil-body Structural Proteins, Oleosin and Caleosin, in Castor Bean and Flax." Gene, vol. 515, no. 2, 2013, pp. 454-60.
Hyun TK, Kumar D, Cho YY, et al. Computational identification and phylogenetic analysis of the oil-body structural proteins, oleosin and caleosin, in castor bean and flax. Gene. 2013;515(2):454-60.
Hyun, T. K., Kumar, D., Cho, Y. Y., Hyun, H. N., & Kim, J. S. (2013). Computational identification and phylogenetic analysis of the oil-body structural proteins, oleosin and caleosin, in castor bean and flax. Gene, 515(2), 454-60. https://doi.org/10.1016/j.gene.2012.11.065
Hyun TK, et al. Computational Identification and Phylogenetic Analysis of the Oil-body Structural Proteins, Oleosin and Caleosin, in Castor Bean and Flax. Gene. 2013 Feb 25;515(2):454-60. PubMed PMID: 23232356.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Computational identification and phylogenetic analysis of the oil-body structural proteins, oleosin and caleosin, in castor bean and flax. AU - Hyun,Tae Kyung, AU - Kumar,Dhinesh, AU - Cho,Young-Yeol, AU - Hyun,Hae-Nam, AU - Kim,Ju-Sung, Y1 - 2012/12/08/ PY - 2012/03/12/received PY - 2012/07/05/revised PY - 2012/11/29/accepted PY - 2012/12/13/entrez PY - 2012/12/13/pubmed PY - 2013/3/27/medline SP - 454 EP - 60 JF - Gene JO - Gene VL - 515 IS - 2 N2 - Oil bodies (OBs) are the intracellular particles derived from oilseeds. These OBs store lipids as a carbon resource, and have been exploited for a variety of industrial applications including biofuels. Oleosin and caleosin are the common OB structural proteins which are enabling biotechnological enhancement of oil content and OB-based pharmaceutical formations via stabilizing OBs. Although the draft whole genome sequence information for Ricinus communis L. (castor bean) and Linum usitatissimum L. (flax), important oil seed plants, is available in public database, OB-structural proteins in these plants are poorly indentified. Therefore, in this study, we performed a comprehensive bioinformatic analysis including analysis of the genome sequence, conserved domains and phylogenetic relationships to identify OB structural proteins in castor bean and flax genomes. Using comprehensive analysis, we have identified 6 and 15 OB-structural proteins from castor bean and flax, respectively. A complete overview of this gene family in castor bean and flax is presented, including the gene structures, phylogeny and conserved motifs, resulting in the presence of central hydrophobic regions with proline knot motif, providing an evolutionary proof that this central hydrophobic region had evolved from duplications in the primitive eukaryotes. In addition, expression analysis of L-oleosin and caleosin genes using quantitative real-time PCR demonstrated that seed contained their maximum expression, except that RcCLO-1 expressed maximum in cotyledon. Thus, our comparative genomics analysis of oleosin and caleosin genes and their putatively encoded proteins in two non-model plant species provides insights into the prospective usage of gene resources for improving OB-stability. SN - 1879-0038 UR - https://www.unboundmedicine.com/medline/citation/23232356/Computational_identification_and_phylogenetic_analysis_of_the_oil_body_structural_proteins_oleosin_and_caleosin_in_castor_bean_and_flax_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0378-1119(12)01486-2 DB - PRIME DP - Unbound Medicine ER -