A5084313216- Peroxisome Proliferator-Activated Receptors
- RNA Research and Splicing
- ATP Synthase and ATPases Research
- Photoreceptor and optogenetics research
- Photosynthetic Processes and Mechanisms
- Prion Diseases and Protein Misfolding
- RNA modifications and cancer
- Retinal Development and Disorders
- Genetics, Aging, and Longevity in Model Organisms
- Spaceflight effects on biology
- Fungal and yeast genetics research
- Protein Degradation and Inhibitors
- Endoplasmic Reticulum Stress and Disease
- RNA and protein synthesis mechanisms
- Neurological diseases and metabolism
- Nuclear Receptors and Signaling
- Circadian rhythm and melatonin
- Signaling Pathways in Disease
University of California, Berkeley
2018-2025
QB3
2020-2025
Ursinus College
2014-2017
Berkeley College
2015
University of California System
2015
Pex1 and Pex6 form a heterohexameric motor essential for peroxisome biogenesis function, mutations in these AAA-ATPases cause most peroxisome-biogenesis disorders humans. The tail-anchored protein Pex15 recruits Pex1/Pex6 to the peroxisomal membrane, where it performs an unknown function required matrix-protein import. Here we determine that from S. cerevisiae is translocase unfolds pore-loop-dependent ATP-hydrolysis-dependent manner. Our structural studies of isolation complex with...
Abstract Recent work has demonstrated that the soluble photoconvertable fluorescent protein mEOS can be a reporter for AAA+ (ATPases Associated with diverse cellular Activities) unfoldase activity. Given many proteins process membrane proteins, we sought to adapt use substrates. However, direct genetic fusion of completely abolished fluorescence, severely limiting utility studying proteins. To circumvent this challenge, separately purified and degron, covalently linked them via Sortase,...
Recent work has demonstrated that the soluble photoconvertable fluorescent protein mEOS can be a reporter for AAA+ (ATPases Associated with diverse cellular Activities) unfoldase activity. Given many proteins process membrane proteins, we sought to adapt use substrates. However, direct genetic fusion of completely abolished fluorescence, severely limiting utility studying proteins. To circumvent this challenge, separately purified and multiple different degrons, including transmembrane...
The number of known fungal proteins capable switching between alternative stable conformations is steadily increasing, suggesting that a prion-like mechanism may be broadly utilized as means to propagate altered cellular states. To gain insight into the mechanisms by which cells regulate prion formation and toxicity we examined role yeast ribosome-associated complex (RAC) in modulating both [PSI+] – an conformer Sup35 protein aggregation-prone polypeptides. Hsp40 RAC chaperone Zuo1 anchors...
Significance The AAA+ ATPase Msp1 has previously been shown to function in the quality control of tail-anchored proteins at mitochondrial and peroxisomal membranes, yet its detailed mechanisms substrate processing have remained unknown. Using scaffolds stabilize functional hexamer domains various model derived from Msp1’s endogenous Pex15, we show that is a promiscuous protein translocase mechanically unfolds pulls substrates through central pore an N-to-C or C-to-N terminal direction. Pex3...
The heterohexameric ATPases associated with diverse cellular activities (AAA)-ATPase Pex1/Pex6 is essential for the formation and maintenance of peroxisomes. Pex1/Pex6, similar to other AAA-ATPases, uses energy from ATP hydrolysis mechanically thread substrate proteins through its central pore, thereby unfolding them. In related AAA-ATPase motors, substrates are recruited binding motor's N-terminal domains or N terminally bound cofactors. Here, we use structural biochemical techniques...
The heterohexameric AAA-ATPase Pex1/Pex6 is essential for the formation and maintenance of peroxisomes. Pex1/Pex6, similar to other AAA-ATPases, uses energy from ATP hydrolysis mechanically thread substrate proteins through its central pore, thereby unfolding them. In related motors, substrates are recruited binding motor's N-terminal domains or N-terminally bound co-factors. Here we use structural biochemical techniques characterize function N1 domain in Pex6 budding yeast, S. cerevisiae....
Prions are self‐propagating infectious protein conformations. In mammals prions underlie the transmissible spongiform encephalopathies, a set of invariably fatal neurodegenerative disorders associated with misfolding mammalian prion protein, PrP. recent years increasing numbers fungal proteins capable infectiously propagating altered conformations have been discovered. Fungal typically not lethal and debate continues as to whether they may evolutionarily conserved physiological roles rather...
The heterohexameric AAA-ATPase Pex1/Pex6 is essential for the formation and maintenance of peroxisomes. Pex1/Pex6, similar to other AAA-ATPases, uses energy from ATP hydrolysis mechanically thread substrate proteins through its central pore, thereby unfolding them. In related motors, substrates are recruited binding motor's N-terminal domains or N-terminally bound co-factors. Here we use structural biochemical techniques characterize function N1 domain in Pex6 budding yeast,