English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/147802
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47

AuthorsGuerra-Castellano, Alejandra ; Díaz-Moreno, Irene ; Velázquez-Campoy, Adrián; Rosa, Miguel A. de la ; Díaz-Quintana, Antonio
KeywordsCaspase activity
Cytochrome c
Electron transport chain
Liposomes binding
Peroxidase activity
Phosphorylation
Issue Date2016
PublisherElsevier
CitationBiochimica et Biophysica Acta - Bioenergetics 1857(4): 387-395 (2016)
AbstractProtein function is frequently modulated by post-translational modifications of specific residues. Cytochrome c, in particular, is phosphorylated in vivo at threonine 28 and serine 47. However, the effect of such modifications on the physiological functions of cytochrome c – namely, the transfer of electrons in the respiratory electron transport chain and the triggering of programmed cell death – is still unknown. Here we replace each of these two residues by aspartate, in order to mimic phosphorylation, and report the structural and functional changes in the resulting cytochrome c variants. We find that the T28D mutant causes a 30-mV decrease on the midpoint redox potential and lowers the affinity for the distal site of Arabidopsis thaliana cytochrome c1 in complex III. Both the T28D and S47D variants display a higher efficiency as electron donors for the cytochrome c oxidase activity of complex IV. In both protein mutants, the peroxidase activity is significantly higher, which is related to the ability of cytochrome c to leave the mitochondria and reach the cytoplasm. We also find that both mutations at serine 47 (S47D and S47A) impair the ability of cytoplasmic cytochrome c to activate the caspases cascade, which is essential for triggering programmed cell death.
Publisher version (URL)http://dx.doi.org/10.1016/j.bbabio.2016.01.011
URIhttp://hdl.handle.net/10261/147802
DOI10.1016/j.bbabio.2016.01.011
Appears in Collections:(IBVF) Artículos
Files in This Item:
File Description SizeFormat 
BBA 2016.pdf1,09 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.