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Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds.
Plant Cell Physiol. 1999 Oct; 40(10):1079-86.PC

Abstract

Plant seed oil bodies comprise a matrix of triacylglycerols surrounded by a monolayer of phospholipids embedded with abundant oleosins and some minor proteins. Three minor proteins, temporarily termed Sops 1-3, have been identified in sesame oil bodies. A cDNA sequence of Sop1 was obtained by PCR cloning using degenerate primers derived from two partial amino acid sequences, and subsequently confirmed via immunological recognition of its over-expressed protein in Escherichia coli. Alignment with four published homologous sequences suggests Sop1 as a putative calcium-binding protein. Immunological cross-recognition implies that this protein, tentatively named caleosin, exists in diverse seed oil bodies. Caleosin migrated faster in SDS-PAGE when incubated with Ca2+. A single copy of caleosin gene was found in sesame genome based on Southern hybridization. Northern hybridization revealed that both caleosin and oleosin genes were concurrently transcribed in maturing seeds where oil bodies are actively assembled. Hydropathy plot and secondary structure analysis suggest that caleosin comprises three structural domains, i.e., an N-terminal hydrophilic calcium-binding domain, a central hydrophobic anchoring domain, and a C-terminal hydrophilic phosphorylation domain. Compared with oleosin, a conserved proline knot-like motif is located in the central hydrophobic domain of caleosin and assumed to involve in protein assembly onto oil bodies.

Authors+Show Affiliations

Graduate Institute of Agricultural Biotechnology, National Chung-Hsing University, Taichung, Taiwan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10589521

Citation

Chen, J C., et al. "Cloning and Secondary Structure Analysis of Caleosin, a Unique Calcium-binding Protein in Oil Bodies of Plant Seeds." Plant & Cell Physiology, vol. 40, no. 10, 1999, pp. 1079-86.
Chen JC, Tsai CC, Tzen JT. Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds. Plant Cell Physiol. 1999;40(10):1079-86.
Chen, J. C., Tsai, C. C., & Tzen, J. T. (1999). Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds. Plant & Cell Physiology, 40(10), 1079-86.
Chen JC, Tsai CC, Tzen JT. Cloning and Secondary Structure Analysis of Caleosin, a Unique Calcium-binding Protein in Oil Bodies of Plant Seeds. Plant Cell Physiol. 1999;40(10):1079-86. PubMed PMID: 10589521.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds. AU - Chen,J C, AU - Tsai,C C, AU - Tzen,J T, PY - 1999/12/10/pubmed PY - 1999/12/10/medline PY - 1999/12/10/entrez SP - 1079 EP - 86 JF - Plant & cell physiology JO - Plant Cell Physiol VL - 40 IS - 10 N2 - Plant seed oil bodies comprise a matrix of triacylglycerols surrounded by a monolayer of phospholipids embedded with abundant oleosins and some minor proteins. Three minor proteins, temporarily termed Sops 1-3, have been identified in sesame oil bodies. A cDNA sequence of Sop1 was obtained by PCR cloning using degenerate primers derived from two partial amino acid sequences, and subsequently confirmed via immunological recognition of its over-expressed protein in Escherichia coli. Alignment with four published homologous sequences suggests Sop1 as a putative calcium-binding protein. Immunological cross-recognition implies that this protein, tentatively named caleosin, exists in diverse seed oil bodies. Caleosin migrated faster in SDS-PAGE when incubated with Ca2+. A single copy of caleosin gene was found in sesame genome based on Southern hybridization. Northern hybridization revealed that both caleosin and oleosin genes were concurrently transcribed in maturing seeds where oil bodies are actively assembled. Hydropathy plot and secondary structure analysis suggest that caleosin comprises three structural domains, i.e., an N-terminal hydrophilic calcium-binding domain, a central hydrophobic anchoring domain, and a C-terminal hydrophilic phosphorylation domain. Compared with oleosin, a conserved proline knot-like motif is located in the central hydrophobic domain of caleosin and assumed to involve in protein assembly onto oil bodies. SN - 0032-0781 UR - https://www.unboundmedicine.com/medline/citation/10589521/Cloning_and_secondary_structure_analysis_of_caleosin_a_unique_calcium_binding_protein_in_oil_bodies_of_plant_seeds_ L2 - https://academic.oup.com/pcp/article-lookup/doi/10.1093/oxfordjournals.pcp.a029490 DB - PRIME DP - Unbound Medicine ER -