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| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | González Montoro, María Ayelén | - |
| dc.creator | Quiroga, Rodrigo | - |
| dc.creator | Valdez, Javier Esteban | - |
| dc.date | 2017-10-04T19:27:27Z | - |
| dc.date | 2017-10-04T19:27:27Z | - |
| dc.date | 2013-09 | - |
| dc.date | 2017-10-03T18:22:55Z | - |
| dc.date.accessioned | 2019-04-29T15:39:03Z | - |
| dc.date.available | 2019-04-29T15:39:03Z | - |
| dc.date.issued | 2013-09 | - |
| dc.identifier | González Montoro, María Ayelén; Quiroga, Rodrigo; Valdez, Javier Esteban; Zinc co-ordination by the DHHC cysteine-rich domain of the palmitoyltransferase Swf1; Portland Press; Biochemical Journal; 454; 3; 9-2013; 427-435 | - |
| dc.identifier | 0264-6021 | - |
| dc.identifier | http://hdl.handle.net/11336/25900 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298557 | - |
| dc.description | S-acylation, commonly known as palmitoylation, is a widespread post-translational modification of proteins that consists of the thioesterification of one or more cysteine residues with fatty acids. This modification is catalysed by a family of PATs (palmitoyltransferases), characterized by the presence of a 50-residue long DHHC-CRD (Asp-His-His-Cys cysteinerich domain). To gain knowledge on the structure–function relationships of these proteins, we carried out a randommutagenesis assay designed to uncover essential amino acids in Swf1, the yeast PAT responsible for the palmitoylation of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins. We identified 21 novel loss-of-function mutations, which are mostly localized within the DHHC-CRD. Modelling of the tertiary structure of the Swf1 DHHC domain suggests that it could fold as a zinc-finger domain, co-ordinating two zinc atoms in a CCHC arrangement. All residues predicted to be involved in the co-ordination of zinc were found to be essential for Swf1 function in the screen. Moreover, these mutations result in unstable proteins, in agreement with a structural role for these zinc fingers. The conservation of amino acids predicted to form each zinc-binding pocket suggests a shared function, as the selective pressure to maintain them is lost upon mutation of one of them. A Swf1 orthologue that lacks one of the zinc-binding pockets is able to complement a yeast swf1Δ strain, possibly because a similar fold can be stabilized by hydrogen bonds instead of zinc co-ordination. Finally, we show directly that recombinant Swf1 DHHC-CRD is able to bind zinc. Sequence analyses of DHHC domains allowed us to present models of the zinc-binding properties for all PATs. | - |
| dc.description | Fil: González Montoro, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina | - |
| dc.description | Fil: Quiroga, Rodrigo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina | - |
| dc.description | Fil: Valdez, Javier Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Portland Press | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1042/BJ20121693 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.biochemj.org/content/454/3/427 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/25900 | - |
| dc.subject | S-acylation | - |
| dc.subject | Protein | - |
| dc.subject | DHCC domain | - |
| dc.subject | Zinc coordination | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Zinc co-ordination by the DHHC cysteine-rich domain of the palmitoyltransferase Swf1 | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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