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The multigene family of lysophosphatidate acyltransferase (LPAT)-related enzymes in Ricinus communis: cloning and molecular characterization of two LPAT genes that are expressed in castor seeds.
Plant Sci. 2013 Feb; 199-200:29-40.PS

Abstract

The multigene family encoding proteins related to lysophosphatidyl-acyltransferases (LPATs) has been analyzed in the castor plant Ricinus communis. Among them, two genes designated RcLPAT2 and RcLPATB, encoding proteins with LPAT activity and expressed in the developing seed, have been cloned and characterized in some detail. RcLPAT2 groups with well characterized members of the so-called A-class LPATs and it shows a generalized expression pattern in the plant and along seed development. Enzymatic assays of RcLPAT2 indicate a preference for ricinoleoyl-CoA over other fatty acid thioesters when ricinoleoyl-LPA is used as the acyl acceptor, while oleoyl-CoA is the preferred substrate when oleoyl-LPA is employed. RcLPATB groups with B-class LPAT enzymes described as seed specific and selective for unusual fatty acids. However, RcLPATB exhibit a broad specificity on the acyl-CoAs, with saturated fatty acids (12:0-16:0) being the preferred substrates. RcLPATB is upregulated coinciding with seed triacylglycerol accumulation, but its expression is not restricted to the seed. These results are discussed in the light of a possible role for LPAT isoenzymes in the channelling of ricinoleic acid into castor bean triacylglycerol.

Authors+Show Affiliations

Grupo de Biotecnología de Productos Naturales (BIO-279), Centro de Investigación en Biotecnología Agroalimentaria, Campus de Excelencia Internacional Agroalimentario (CeiA3), Universidad de Almería, Almería, Spain.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

23265316

Citation

Arroyo-Caro, José María, et al. "The Multigene Family of Lysophosphatidate Acyltransferase (LPAT)-related Enzymes in Ricinus Communis: Cloning and Molecular Characterization of Two LPAT Genes That Are Expressed in Castor Seeds." Plant Science : an International Journal of Experimental Plant Biology, vol. 199-200, 2013, pp. 29-40.
Arroyo-Caro JM, Chileh T, Kazachkov M, et al. The multigene family of lysophosphatidate acyltransferase (LPAT)-related enzymes in Ricinus communis: cloning and molecular characterization of two LPAT genes that are expressed in castor seeds. Plant Sci. 2013;199-200:29-40.
Arroyo-Caro, J. M., Chileh, T., Kazachkov, M., Zou, J., Alonso, D. L., & García-Maroto, F. (2013). The multigene family of lysophosphatidate acyltransferase (LPAT)-related enzymes in Ricinus communis: cloning and molecular characterization of two LPAT genes that are expressed in castor seeds. Plant Science : an International Journal of Experimental Plant Biology, 199-200, 29-40. https://doi.org/10.1016/j.plantsci.2012.09.015
Arroyo-Caro JM, et al. The Multigene Family of Lysophosphatidate Acyltransferase (LPAT)-related Enzymes in Ricinus Communis: Cloning and Molecular Characterization of Two LPAT Genes That Are Expressed in Castor Seeds. Plant Sci. 2013;199-200:29-40. PubMed PMID: 23265316.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The multigene family of lysophosphatidate acyltransferase (LPAT)-related enzymes in Ricinus communis: cloning and molecular characterization of two LPAT genes that are expressed in castor seeds. AU - Arroyo-Caro,José María, AU - Chileh,Tarik, AU - Kazachkov,Michael, AU - Zou,Jitao, AU - Alonso,Diego López, AU - García-Maroto,Federico, Y1 - 2012/11/10/ PY - 2012/07/23/received PY - 2012/09/14/revised PY - 2012/09/16/accepted PY - 2012/12/26/entrez PY - 2012/12/26/pubmed PY - 2013/6/5/medline SP - 29 EP - 40 JF - Plant science : an international journal of experimental plant biology JO - Plant Sci VL - 199-200 N2 - The multigene family encoding proteins related to lysophosphatidyl-acyltransferases (LPATs) has been analyzed in the castor plant Ricinus communis. Among them, two genes designated RcLPAT2 and RcLPATB, encoding proteins with LPAT activity and expressed in the developing seed, have been cloned and characterized in some detail. RcLPAT2 groups with well characterized members of the so-called A-class LPATs and it shows a generalized expression pattern in the plant and along seed development. Enzymatic assays of RcLPAT2 indicate a preference for ricinoleoyl-CoA over other fatty acid thioesters when ricinoleoyl-LPA is used as the acyl acceptor, while oleoyl-CoA is the preferred substrate when oleoyl-LPA is employed. RcLPATB groups with B-class LPAT enzymes described as seed specific and selective for unusual fatty acids. However, RcLPATB exhibit a broad specificity on the acyl-CoAs, with saturated fatty acids (12:0-16:0) being the preferred substrates. RcLPATB is upregulated coinciding with seed triacylglycerol accumulation, but its expression is not restricted to the seed. These results are discussed in the light of a possible role for LPAT isoenzymes in the channelling of ricinoleic acid into castor bean triacylglycerol. SN - 1873-2259 UR - https://www.unboundmedicine.com/medline/citation/23265316/The_multigene_family_of_lysophosphatidate_acyltransferase__LPAT__related_enzymes_in_Ricinus_communis:_cloning_and_molecular_characterization_of_two_LPAT_genes_that_are_expressed_in_castor_seeds_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0168-9452(12)00223-3 DB - PRIME DP - Unbound Medicine ER -