A5073111934- Mitochondrial Function and Pathology
- Coenzyme Q10 studies and effects
- Heat shock proteins research
- Protein Structure and Dynamics
- Advanced battery technologies research
- Neurological diseases and metabolism
- Genetic Neurodegenerative Diseases
- Organic Chemistry Cycloaddition Reactions
- Fungal and yeast genetics research
- Enzyme Structure and Function
- Biochemical Acid Research Studies
- Metabolism and Genetic Disorders
- Metalloenzymes and iron-sulfur proteins
Morgridge Institute for Research
2021-2022
Washington University in St. Louis
2021-2022
Gdańsk Medical University
2014-2015
University of Gdańsk
2013
Abstract Beyond its role in mitochondrial bioenergetics, Coenzyme Q (CoQ, ubiquinone) serves as a key membrane-embedded antioxidant throughout the cell. However, how CoQ is mobilized from site of synthesis on inner membrane to other sites action remains longstanding mystery. Here, using combination Saccharomyces cerevisiae genetics, biochemical fractionation, and lipid profiling, we identify two highly conserved but poorly characterized proteins, Ypl109c (Cqd1) Ylr253w (Cqd2), that...
Biogenesis of iron–sulfur clusters (FeS) is a highly conserved process involving Hsp70 and J-protein chaperones. However, specialization differs among species. In most eukaryotes, including Schizosaccharomyces pombe, FeS biogenesis involves interaction between the Jac1 multifunctional Ssc1. But, in Saccharomyces cerevisiae closely related species, interacts with specialized Ssq1, which emerged through duplication SSC1. As little known about how gene duplicates affect robustness their protein...
Faithful replication and propagation of mitochondrial DNA (mtDNA) is critical for cellular respiration. Molecular chaperones, ubiquitous proteins involved in protein folding remodeling complexes, have been implicated mtDNA transactions. In particular, cells lacking Mdj1, an Hsp40 co-chaperone Hsp70 the matrix, do not maintain functional mtDNA. Here we report that great majority Mdj1 associated with nucleoids, DNA-protein complexes are unit Underscoring importance chaperone activity...
Abstract Coenzyme Q (CoQ, ubiquinone) is a redox-active lipid essential for core metabolic pathways and antioxidant defense. CoQ synthesized upon the mitochondrial inner membrane by an ill-defined ‘complex Q’ metabolon. Here we present structure functional analyses of substrate- NADH-bound oligomeric complex comprised two subunits: hydroxylase COQ7, which performs penultimate step in biosynthesis, prenyl lipid-binding protein COQ9. We reveal that COQ7 adopts modified ferritin-like fold with...