A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily

dc.creatorSanchez Granel, María L.
dc.creatorSiburu, Nicolás G.
dc.creatorFricska, Annamária
dc.creatorMaldonado, Lucas L.
dc.creatorGargiulo, Laura B.
dc.creatorNudel, Clara B.
dc.creatorUttaro, Antonio Domingo
dc.creatorNusblat, Alejandro D.
dc.date2022-12-15T17:32:40Z
dc.date2022-12-15T17:32:40Z
dc.date2022-10
dc.date2022-12-15T17:32:40Z
dc.date2022-12-15T17:32:40Z
dc.date2022-10
dc.date.accessioned2023-08-30T21:17:30Z
dc.date.available2023-08-30T21:17:30Z
dc.identifier0021-9258
dc.identifierhttp://hdl.handle.net/2133/25032
dc.identifierhttp://hdl.handle.net/2133/25032
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8541927
dc.descriptionSterols in eukaryotic cells play important roles in modulating membrane fluidity and in cell signaling and trafficking. During evolution, a combination of gene losses and acquisitions gave rise to an extraordinary diversity of sterols in different organisms. The sterol C-22 desaturase identified in plants and fungi as a cytochrome P-450 monooxygenase evolved from the first eukaryotic cytochrome P450 and was lost in many lineages. Although the ciliate Tetrahymena thermophila desaturates sterols at the C-22 position, no cytochrome P-450 orthologs are present in the genome. Here, we aim to identify the genes responsible for the desaturation as well as their probable origin. We used gene knockout and yeast heterologous expression approaches to identify two putative genes, retrieved from a previous transcriptomic analysis, as sterol C-22 desaturases. Furthermore, we demonstrate using bioinformatics and evolutionary analyses that both genes encode a novel type of sterol C-22 desaturase that belongs to the large fatty acid hydroxylase/desaturase superfamily and the genes originated by genetic duplication prior to functional diversification. These results stress the widespread existence of nonhomologous isofunctional enzymes among different lineages of the tree of life as well as the suitability for the use of T. thermophila as a valuable model to investigate the evolutionary process of large enzyme families.
dc.descriptionFil: Sanchez Granel, María L. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (UBA-CONICET); Argentina.
dc.descriptionFil: Fricska, Annamária. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (UBA-CONICET); Argentina.
dc.descriptionFil: Gargiulo, Laura B. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (UBA-CONICET); Argentina.
dc.descriptionFil: Nudel, Clara B. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (UBA-CONICET); Argentina.
dc.descriptionFil: Nusblat, Alejandro D. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (UBA-CONICET); Argentina.
dc.descriptionFil: Siburu, Nicolás G. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.descriptionFil: Uttaro, Antonio Domingo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.descriptionFil: Maldonado, Lucas L. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica (UBA-CONICET); Argentina.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.relationhttps://doi.org/10.1016/j.jbc.2022.102397
dc.relationhttps://www.sciencedirect.com/science/article/pii/S0021925822008407?via%3Dihub#coi0010
dc.rightshttp://creativecommons.org/licenses/by/4.0/
dc.rightsSanchez Granel, María L.
dc.rightsSiburu, Nicolás G.
dc.rightsFricska, Annamária
dc.rightsMaldonado, Lucas L.
dc.rightsGargiulo, Laura B.
dc.rightsNudel, Clara B.
dc.rightsUttaro, Antonio Domingo
dc.rightsNusblat, Alejandro D.
dc.rightsAttribution 4.0 International (CC BY 4.0)
dc.rightsopenAccess
dc.subjectCholesterol
dc.subjectSterols
dc.subjectCytochrome P450
dc.subjectLipid
dc.subjectProtein evolution
dc.subjectFatty acid
dc.subjectEndoplasmic reticulum
dc.titleA novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily
dc.typearticle
dc.typeartículo


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