A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily
Sterols 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 i...
Autores principales: | , , , , , , , |
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Lenguaje: | Inglés |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | http://hdl.handle.net/2133/25032 http://hdl.handle.net/2133/25032 |
Aporte de: |
id |
I15-R121-2133-25032 |
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record_format |
dspace |
institution |
Universidad Nacional de Rosario |
institution_str |
I-15 |
repository_str |
R-121 |
collection |
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) |
language |
Inglés |
topic |
Cholesterol Sterols Cytochrome P450 Lipid Protein evolution Fatty acid Endoplasmic reticulum |
spellingShingle |
Cholesterol Sterols Cytochrome P450 Lipid Protein evolution Fatty acid Endoplasmic reticulum Sanchez Granel, María L. Siburu, Nicolás G. Fricska, Annamária Maldonado, Lucas L. Gargiulo, Laura B. Nudel, Clara B. Uttaro, Antonio Domingo Nusblat, Alejandro D. A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
topic_facet |
Cholesterol Sterols Cytochrome P450 Lipid Protein evolution Fatty acid Endoplasmic reticulum |
description |
Sterols 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. |
author |
Sanchez Granel, María L. Siburu, Nicolás G. Fricska, Annamária Maldonado, Lucas L. Gargiulo, Laura B. Nudel, Clara B. Uttaro, Antonio Domingo Nusblat, Alejandro D. |
author_facet |
Sanchez Granel, María L. Siburu, Nicolás G. Fricska, Annamária Maldonado, Lucas L. Gargiulo, Laura B. Nudel, Clara B. Uttaro, Antonio Domingo Nusblat, Alejandro D. |
author_sort |
Sanchez Granel, María L. |
title |
A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
title_short |
A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
title_full |
A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
title_fullStr |
A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
title_full_unstemmed |
A novel Tetrahymena thermophila sterol C-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
title_sort |
novel tetrahymena thermophila sterol c-22 desaturase belongs to the fatty acid hydroxylase/desaturase superfamily |
publisher |
Elsevier |
publishDate |
2022 |
url |
http://hdl.handle.net/2133/25032 http://hdl.handle.net/2133/25032 |
work_keys_str_mv |
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bdutipo_str |
Repositorios |
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