ArticleProceedings of the National Academy of Sciences of the United States of America2019
Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.Communications biology · 2025Article
- Molecular adaptations specific to extreme halophilic archaea could promote high perchlorate tolerance.Applied and environmental microbiology · 2025Article
- DiffModeler: large macromolecular structure modeling for cryo-EM maps using a diffusion model.Nature methods · 2024Article
- ProEnd: a comprehensive database for identifying HbYX motif-containing proteins across the tree of life.BMC genomics · 2024Article
- Article
- ProEnd: A Comprehensive Database for Identifying HbYX Motif-Containing Proteins Across the Tree of Life.bioRxiv : the preprint server for biology · 2024Article
- DiffModeler: Large Macromolecular Structure Modeling in Low-Resolution Cryo-EM Maps Using Diffusion Model.bioRxiv : the preprint server for biology · 2024Article
- A concerted ATPase cycle of the protein transporter AAA-ATPase Bcs1.Nature communications · 2023Article
- A Role for the Proteasome Alpha2 Subunit N-Tail in Substrate Processing.Biomolecules · 2023Article
- Bortezomib advanced mechanisms of action in multiple myeloma, solid and liquid tumors along with its novel therapeutic applications.EXCLI journal · 2023Review
- Matrix-Landing Mass Spectrometry for Electron Microscopy Imaging of Native Protein Complexes.Analytical chemistry · 2022Article
- Article
- Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.Molecular microbiology · 2022Article
- Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules.The Journal of biological chemistry · 2022Review
- The YΦ motif defines the structure-activity relationships of human 20S proteasome activators.Nature communications · 2022Article
- An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation.eLife · 2022Article
- Targeting Proteasomes in Cancer and Infectious Disease: A Parallel Strategy to Treat Malignancies and Microbes.Frontiers in cellular and infection microbiology · 2022Review
- Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines.Biophysical journal · 2021Article
- Simulating the directional translocation of a substrate by the AAA+ motor in the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.
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