In mitochondria, the major subunits of oxidative phosphorylation complexes are translated by the mitochondrial ribosome (mito-ribosome). The correct insertion and assembly of these subunits into the inner mitochondrial membrane (IMM) are facilitated by mitochondrial oxidase assembly protein 1 (Oxa1) during the translation process. This co-translational insertion process involves an association between the mito-ribosome and the C-terminus of Oxa1 (Oxa1-CTD) Nuclear magnetic resonance (NMR)...
[NMR paper] NMR and Patch-Clamp Characterization of Yeast Mitochondrial Pyruvate Carrier Complexes
NMR and Patch-Clamp Characterization of Yeast Mitochondrial Pyruvate Carrier Complexes
The mitochondrial pyruvate carrier (Mpc) plays an indispensable role in the transport of pyruvates across the mitochondrial inner membrane. Despite the two distinct homologous proteins, Mpc1 and Mpc2, were identified in 2012, there are still controversies on the basic functional units and oligomeric state of Mpc complexes. In this study, yeast Mpc1 and Mpc2 proteins were expressed in a prokaryotic heterologous system. Both homo- and hetero-dimers were successfully reconstituted in mixed...
More...
nmrlearner
Journal club
0
05-27-2023 02:53 PM
[NMR paper] NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP
NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP
CONCLUSIONS: Together with functional analysis of purified CytcO, we suggest that this ATP interaction is inhibitory of catalytic activity. Our results shed light on the structural flexibility of an important subunit of yeast CytcO and provide structure-based insight into how ATP could regulate mitochondrial respiration.
More...
nmrlearner
Journal club
0
05-13-2021 07:58 PM
[ASAP] In vitro-Constructed Ribosomes Enable Multi-site Incorporation of Noncanonical Amino Acids into Proteins
In vitro-Constructed Ribosomes Enable Multi-site Incorporation of Noncanonical Amino Acids into Proteins
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00829/20210111/images/medium/bi0c00829_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00829
http://feeds.feedburner.com/~r/acs/bichaw/~4/ka6wq8GcKfY
More...
nmrlearner
Journal club
0
01-13-2021 08:38 AM
[NMR paper] The NMR-based characterization of the FTY720-SET complex reveals an alternative mechanism for the attenuation of the inhibitory SET-PP2A interaction.
The NMR-based characterization of the FTY720-SET complex reveals an alternative mechanism for the attenuation of the inhibitory SET-PP2A interaction.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.fasebj.org-pb-assets-images-faseb-pubmed-logo.gif The NMR-based characterization of the FTY720-SET complex reveals an alternative mechanism for the attenuation of the inhibitory SET-PP2A interaction.
FASEB J. 2019 Mar 27;:fj201802264R
Authors: De Palma RM, Parnham SR, Li Y, Oaks JJ, Peterson YK, Szulc ZM, Roth BM, Xing Y,...
nmrlearner
Journal club
0
03-30-2019 05:11 AM
[NMR paper] Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
J Biomol NMR. 2013 May 25;
Authors: Volkov AN, van Nuland NA
Abstract
Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution....
nmrlearner
Journal club
0
05-28-2013 06:36 PM
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
Abstract The application of metabolomics to human and animal model systems is poised to provide great insight into our understanding of disease etiology and the metabolic changes that are associated with these conditions. However, metabolomic studies have also revealed that there is significant, inherent biological variation in human samples and even in samples from animal model systems where the animals are housed under carefully controlled conditions. This inherent biological...
nmrlearner
Journal club
0
03-03-2011 02:06 AM
[NMR paper] Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidiz
Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR.
Related Articles Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR.
Biochemistry. 2003 Dec 9;42(48):14139-49
Authors: Trivelli X, Krimm I, Ebel C, Verdoucq L, Prouzet-Mauléon V, Chartier Y, Tsan P, Lauquin G, Meyer Y, Lancelin JM
Peroxiredoxins (Prx's) are a superfamily of thiol-specific antioxidant proteins present in all organisms and involved in the hydroperoxide...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
Related Articles Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
Biochemistry. 2001 Jun 19;40(24):7069-76
Authors: Worrall JA, Kolczak U, Canters GW, Ubbink M
The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both...
NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes
Linear Mode
