ArticleFrontiers in molecular biosciences2017
The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins.
Article in Frontiers in molecular biosciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Rapid adaptation of cellular metabolic rate to the MicroRNA complements of mammals and its relevance to the evolution of endothermy.iScience · 2024Article
- Neuronal membrane proteasome-derived peptides modulate NMDAR-dependent neuronal signaling to promote changes in gene expression.Molecular biology of the cell · 2024Article
- The proteasome and its role in the nervous system.Cell chemical biology · 2021Review
- Phytoplankton trigger the production of cryptic metabolites in the marine actinobacterium Salinispora tropica.Microbial biotechnology · 2021Article
- Mode of targeting to the proteasome determines GFP fate.The Journal of biological chemistry · 2020Article
- Increased AMP deaminase activity decreases ATP content and slows protein degradation in cultured skeletal muscle.Metabolism: clinical and experimental · 2020Article
- Single-molecule imaging analysis reveals the mechanism of a high-catalytic-activity mutant of chitinase A fromThe Journal of biological chemistry · 2020Article
- A Practical Review of Proteasome Pharmacology.Pharmacological reviews · 2019Review
- Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.Frontiers in molecular biosciences · 2019Review
- Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.Nature communications · 2018Article
- The Logic of the 26S Proteasome.Cell · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
All domains of life have ATP-dependent compartmentalized proteases that sequester their peptidase sites on their interior. ATPase complexes will often associate with these compartmentalized proteases in order to unfold and inject substrates into the protease for degradation. Significant effort has been put into understanding how ATP hydrolysis is used to apply force to proteins and cause them to unfold. The unfolding kinetics of the bacterial ATPase, ClpX, have been shown to resemble a fast motor that traps unfolded intermediates as a strategy to unfold proteins. In the present study, we sought to determine if the proteasomal ATPases from eukaryotes and archaea exhibit similar unfolding kinetics. We found that the proteasomal ATPases appear to use a different kinetic strategy for protein unfolding, behaving as a slower but more processive and efficient translocation motor, particularly when encountering a folded domain. We expect that these dissimilarities are due to differences in the ATP binding/exchange cycle, the presence of a trans-arginine finger, or the presence of a threading ring (i.e., the OB domain), which may be used as a rigid platform to pull folded domains against. We speculate that these differences may have evolved due to the differing client pools these machines are expected to encounter.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.