Argentina | Artículos de revistas
dc.creatorTomazic, Mariela Luján
dc.creatorNajle, Sebastián Rodrigo
dc.creatorNusblat, Alejandro David
dc.creatorUttaro, Antonio Domingo
dc.creatorNudel, Berta Clara
dc.date.accessioned2017-07-26T20:43:09Z
dc.date.accessioned2018-11-06T16:16:34Z
dc.date.available2017-07-26T20:43:09Z
dc.date.available2018-11-06T16:16:34Z
dc.date.created2017-07-26T20:43:09Z
dc.date.issued2011-01
dc.identifierTomazic, 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.identifier1535-9778
dc.identifierhttp://hdl.handle.net/11336/21385
dc.identifier1535-9786
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1906413
dc.description.abstractThe 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.languageeng
dc.publisherAmerican Society For Microbiology
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1128/EC.00259-10
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://ec.asm.org/content/10/3/423
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectNOVEL STEROL DESATURASE-LIKE PROTEIN
dc.subjectT. THERMOPHILA
dc.titleA Novel Sterol Desaturase-Like Protein Promoting Dealkylation of Phytosterols in Tetrahymena thermophila
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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