Cargando…
Protein oxidation in the intermembrane space of mitochondria is substrate-specific rather than general
In most cellular compartments cysteine residues are predominantly reduced. However, in the bacterial periplasm, the ER and the mitochondrial intermembrane space (IMS), sulfhydryl oxidases catalyze the formation of disulfide bonds. Nevertheless, many IMS proteins contain reduced cysteines that partic...
Autores principales: | Peleh, Valentina, Riemer, Jan, Dancis, Andrew, Herrmann, Johannes M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Shared Science Publishers OG
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5349226/ https://www.ncbi.nlm.nih.gov/pubmed/28357226 http://dx.doi.org/10.15698/mic2014.01.130 |
Ejemplares similares
-
Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space
por: Kojer, Kerstin, et al.
Publicado: (2015) -
Mia40 is a trans-site receptor that drives protein import into the mitochondrial intermembrane space by hydrophobic substrate binding
por: Peleh, Valentina, et al.
Publicado: (2016) -
Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40
por: Peleh, Valentina, et al.
Publicado: (2017) -
Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria
por: Herrmann, Johannes M., et al.
Publicado: (2007) -
Protein Translocation into the Intermembrane Space and Matrix of Mitochondria: Mechanisms and Driving Forces
por: Backes, Sandra, et al.
Publicado: (2017)