Cargando…
A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import
Tim17 is a central, membrane-embedded subunit of the mitochondrial protein import machinery. In this study, we show that Tim17 contains a pair of highly conserved cysteine residues that form a structural disulfide bond exposed to the intermembrane space (IMS). This disulfide bond is critical for eff...
Autores principales: | Ramesh, Ajay, Peleh, Valentina, Martinez-Caballero, Sonia, Wollweber, Florian, Sommer, Frederik, van der Laan, Martin, Schroda, Michael, Alexander, R. Todd, Campo, María Luisa, Herrmann, Johannes M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4987294/ https://www.ncbi.nlm.nih.gov/pubmed/27502485 http://dx.doi.org/10.1083/jcb.201602074 |
Ejemplares similares
-
Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import
por: Denkert, Niels, et al.
Publicado: (2017) -
Deletion of Mgr2p Affects the Gating Behavior of the TIM23 Complex
por: Mirzalieva, Oygul, et al.
Publicado: (2019) -
Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system
por: Groß, Dominik P., et al.
Publicado: (2011) -
Preventing Voltage-dependent Gating of Anthrax Toxin Channels Using Engineered Disulfides
por: Anderson, Damon S., et al.
Publicado: (2008) -
Investigating the crucial roles of aliphatic tails in disulfide bond-linked docetaxel prodrug nanoassemblies
por: Wang, Yuequan, et al.
Publicado: (2021)