Cu-NirK from Haloferax mediterranei as an example of metalloprotein maturation and exportation via Tat system

Por favor, use este identificador para citar o enlazar este ítem:
Información del item - Informació de l'item - Item information
Título: Cu-NirK from Haloferax mediterranei as an example of metalloprotein maturation and exportation via Tat system
Autor/es: Esclapez Espliego, Julia María | Zafrilla Requena, Basilio | Martínez-Espinosa, Rosa María | Bonete, María-José
Grupo/s de investigación o GITE: Biotecnología de Extremófilos (BIOTECEXTREM)
Centro, Departamento o Servicio: Universidad de Alicante. Departamento de Agroquímica y Bioquímica
Palabras clave: Copper nitrite reductase | Haloferax mediterranei | Tat system | Homologous expression | Protein exportation
Área/s de conocimiento: Bioquímica y Biología Molecular
Fecha de publicación: jun-2013
Editor: Elsevier
Cita bibliográfica: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2013, 1834(6): 1003-1009. doi:10.1016/j.bbapap.2013.03.002
Resumen: The green Cu-NirK from Haloferax mediterranei (Cu-NirK) has been expressed, refolded and retrieved as a trimeric enzyme using an expression method developed for halophilic Archaea. This method utilizes Haloferax volcanii as a halophilic host and an expression vector with a constitutive and strong promoter. The enzymatic activity of recombinant Cu-NirK was detected in both cellular fractions (cytoplasmic fraction and membranes) and in the culture media. The characterization of the enzyme isolated from the cytoplasmic fraction as well as the culture media revealed important differences in the primary structure of both forms indicating that Hfx. mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Hfx. mediterranei sequence indicate that these processes are closely related to the Tat system. Furthermore, the N-terminal sequence of the two Cu-NirK subunits constituting different isoforms revealed that translation of this protein could begin at two different points, identifying two possible start codons. The hypothesis proposed in this work for halophilic Cu-NirK processing and exportation via the Tat system represents the first approximation of this mechanism in the Halobacteriaceae family and in Prokarya in general.
Patrocinador/es: This work was financially supported by research grants from the Ministerio de Ciencia e Innovación and FEDER funds from Spain (BIO2008-00082), Generalitat Valenciana (GV/2011/038) and University of Alicante (GRE09-25).
ISSN: 1570-9639 (Print) | 1878-1454 (Online)
DOI: 10.1016/j.bbapap.2013.03.002
Idioma: eng
Tipo: info:eu-repo/semantics/article
Revisión científica: si
Versión del editor:
Aparece en las colecciones:INV - BIOTECEXTREM - Artículos de Revistas
INV - AppBiochem - Artículos de Revistas

Archivos en este ítem:
Archivos en este ítem:
Archivo Descripción TamañoFormato 
Thumbnail2013_Esclapez_etal_BBA-PAP_final.pdfVersión final (acceso restringido)856,03 kBAdobe PDFAbrir    Solicitar una copia

Todos los documentos en RUA están protegidos por derechos de autor. Algunos derechos reservados.