Argentina
| Artículos de revistas
A Novel Sterol Desaturase-Like Protein Promoting Dealkylation of Phytosterols in Tetrahymena thermophila
dc.creator | Tomazic, Mariela Luján | |
dc.creator | Najle, Sebastián Rodrigo | |
dc.creator | Nusblat, Alejandro David | |
dc.creator | Uttaro, Antonio Domingo | |
dc.creator | Nudel, Berta Clara | |
dc.date.accessioned | 2017-07-26T20:43:09Z | |
dc.date.accessioned | 2018-11-06T16:16:34Z | |
dc.date.available | 2017-07-26T20:43:09Z | |
dc.date.available | 2018-11-06T16:16:34Z | |
dc.date.created | 2017-07-26T20:43:09Z | |
dc.date.issued | 2011-01 | |
dc.identifier | Tomazic, Mariela Luján; Najle, Sebastián Rodrigo; Nusblat, Alejandro David; Uttaro, Antonio Domingo; Nudel, Berta Clara; A Novel Sterol Desaturase-Like Protein Promoting Dealkylation of Phytosterols in Tetrahymena thermophila; American Society For Microbiology; Eukaryotic Cell; 10; 3; 1-2011; 423-434 | |
dc.identifier | 1535-9778 | |
dc.identifier | http://hdl.handle.net/11336/21385 | |
dc.identifier | 1535-9786 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1906413 | |
dc.description.abstract | The gene TTHERM_00438800 (DES24) from the ciliate Tetrahymena thermophila encodes a protein with three conserved histidine clusters, typical of the fatty acid hydroxylase superfamily. Despite its high similarity to sterol desaturase-like enzymes, the phylogenetic analysis groups Des24p in a separate cluster more related to bacterial than to eukaryotic proteins, suggesting a possible horizontal gene transfer event. A somatic knockout of DES24 revealed that the gene encodes a protein, Des24p, which is involved in the dealkylation of phytosterols. Knocked-out mutants were unable to eliminate the C-24 ethyl group from C29 sterols, whereas the ability to introduce other modifications, such as desaturations at positions C-5(6), C-7(8), and C-22(23), were not altered. Although C-24 dealkylations have been described in other organisms, such as insects, neither the enzymes nor the corresponding genes have been identified to date. Therefore, this is the first identification of a gene involved in sterol dealkylation. Moreover, the knockout mutant and wild-type strain differed signifi- cantly in growth and morphology only when cultivated with C29 sterols; under this culture condition, a change from the typical pear-like shape to a round shape and an alteration in the regulation of tetrahymanol biosynthesis were observed. Sterol analysis upon culture with various substrates and inhibitors indicate that the removal of the C-24 ethyl group in Tetrahymena may proceed by a mechanism different from the one currently known. | |
dc.language | eng | |
dc.publisher | American Society For Microbiology | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1128/EC.00259-10 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://ec.asm.org/content/10/3/423 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | NOVEL STEROL DESATURASE-LIKE PROTEIN | |
dc.subject | T. THERMOPHILA | |
dc.title | A Novel Sterol Desaturase-Like Protein Promoting Dealkylation of Phytosterols in Tetrahymena thermophila | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas |