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Artículo

Zinc co-ordination by the DHHC cysteine-rich domain of the palmitoyltransferase Swf1

González Montoro, María AyelénIcon ; Quiroga, RodrigoIcon ; Valdez, Javier EstebanIcon
Fecha de publicación: 09/2013
Editorial: Portland Press
Revista: Biochemical Journal
ISSN: 0264-6021
Idioma: Inglés
Tipo de recurso: Artículo publicado

Resumen

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.
Palabras clave: S-Acylation , Protein , Dhcc Domain , Zinc Coordination
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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
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URI: http://hdl.handle.net/11336/25900
DOI: http://dx.doi.org/10.1042/BJ20121693
URL: http://www.biochemj.org/content/454/3/427
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Articulos(CIQUIBIC) [296]
Articulos de CENTRO DE INVEST.EN QCA.BIOL.DE CORDOBA (P)
Citación
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
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