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

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Title: Cu-NirK from Haloferax mediterranei as an example of metalloprotein maturation and exportation via Tat system
Authors: Esclapez Espliego, Julia María | Zafrilla Requena, Basilio | Martínez-Espinosa, Rosa María | Bonete, María-José
Research Group/s: Biotecnología de Extremófilos (BIOTECEXTREM)
Center, Department or Service: Universidad de Alicante. Departamento de Agroquímica y Bioquímica
Keywords: Copper nitrite reductase | Haloferax mediterranei | Tat system | Homologous expression | Protein exportation
Knowledge Area: Bioquímica y Biología Molecular
Issue Date: Jun-2013
Publisher: Elsevier
Citation: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2013, 1834(6): 1003-1009. doi:10.1016/j.bbapap.2013.03.002
Abstract: 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.
Sponsor: 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).
URI: http://hdl.handle.net/10045/44398
ISSN: 1570-9639 (Print) | 1878-1454 (Online)
DOI: 10.1016/j.bbapap.2013.03.002
Language: eng
Type: info:eu-repo/semantics/article
Peer Review: si
Publisher version: http://dx.doi.org/10.1016/j.bbapap.2013.03.002
Appears in Collections:INV - BIOTECEXTREM - Artículos de Revistas
INV - AppBiochem - Artículos de Revistas

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