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Time line of redox events in aging postmitotic cells
TLDR
The discovery that chronologically aging yeast cells undergo a sudden redox collapse is reported, which affects over 80% of identified thiol-containing proteins, and a time line of events leading up to the system-wide oxidation of the proteome days before cell death is revealed. Expand
Using Quantitative Redox Proteomics to Dissect the Yeast Redoxome*
TLDR
The results suggest that prevailing redox conditions constantly control central cellular pathways by fine-tuning oxidation status and hence activity of these proteins, and provide experimental evidence that the ability of protein thiols to react to changing peroxide levels is likely governed by both thermodynamic and kinetic parameters. Expand
Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked
TLDR
It is shown that the ATPase Get3, which accommodates the hydrophobic tail anchor of clients, has a dual function: promoting tail-anchored protein insertion when glucose is abundant and serving as an ATP-independent holdase chaperone during energy depletion. Expand
Redox regulation of protein folding in the mitochondrial intermembrane space.
TLDR
Novel concepts for assembly of proteins in the intermembrane space, suggesting that this compartment may be similar to that of the endoplasmic reticulum and the prokaryotic periplasm, and new roles in regulation by oxidation-reduction chemistry seem likely to be relevant. Expand
Reconstitution of the mia40-erv1 oxidative folding pathway for the small tim proteins.
TLDR
It is demonstrated that Mia40, Erv1, and oxygen are the minimal machinery for Tim13 oxidation. Expand
Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion
TLDR
Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex and links protein import, assembly, and turnover pathways in the mitochondrion. Expand
Role of Twin Cys-Xaa9-Cys Motif Cysteines in Mitochondrial Import of the Cytochrome c Oxidase Biogenesis Factor Cmc1*
TLDR
The results suggest that the in vitro and in organello oxidative folding of Cmc1, a twin CX9C-containing substrate, which contains an unpaired cysteine, facilitates efficient formation of multiple disulfides and prevents the formation of non-native disulfide bonds. Expand
An approach to crystallizing proteins by synthetic symmetrization
TLDR
Synthetic symmetrization may be a useful approach for enlarging the search space for crystallizing proteins by creating a variety of single-cysteine mutants and yielding numerous novel crystal forms that cannot be realized by monomeric lysozyme. Expand
Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway*
TLDR
Mia40 in mitochondria from the erv1–101 mutant was also trapped in a completely reduced state, demonstrating that Mia40 can accept up to six electrons as substrates are imported, and these studies support that Mia 40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates. Expand
Small Changes: Using Assessment to Direct Instructional Practices in Large-Enrollment Biochemistry Courses
TLDR
Students' performance related to three foundational concepts—hydrogen bonding, bond energy, and pKa—was analyzed and results support the use of assessment data to inform instructional change, especially in large-enrollment classes. Expand
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