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Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.

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Majumder P, Rudack T, Beck F, Danev R, Pfeifer G, Nagy I, Baumeister W
OpenAccess logo Proc Natl Acad Sci U S A 116 534-539 (2019)
Related entries: 6he4, 6he5, 6he7, 6he8, 6he9, 6hea, 6hec

Cited: 43 times
EuropePMC logo PMID: 30559193

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.

Articles - 6hed mentioned but not cited (3)

  1. Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle. Majumder P, Rudack T, Beck F, Danev R, Pfeifer G, Nagy I, Baumeister W. Proc Natl Acad Sci U S A 116 534-539 (2019)
  2. Minimal mechanistic component of HbYX-dependent proteasome activation that reverses impairment by neurodegenerative-associated oligomers. Chuah JJY, Thibaudeau TA, Smith DM. Commun Biol 6 725 (2023)
  3. research-article Minimal mechanistic component of HbYX-dependent proteasome activation. Chuah JJ, Thibaudeau TA, Rexroad MS, Smith DM. Res Sq rs.3.rs-2496767 (2023)


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  22. Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex. Hogrel G, Marino-Puertas L, Laurent S, Ibrahim Z, Covès J, Girard E, Gabel F, Fenel D, Daugeron MC, Clouet-d'Orval B, Basta T, Flament D, Franzetti B. Mol Microbiol 118 16-29 (2022)
  23. Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry. Yu Y, Liu H, Yu Z, Witkowska HE, Cheng Y. Mol Cell Proteomics 19 1997-2015 (2020)
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  26. A concerted ATPase cycle of the protein transporter AAA-ATPase Bcs1. Pan Y, Zhan J, Jiang Y, Xia D, Scheuring S. Nat Commun 14 6369 (2023)
  27. Simulating the conformational dynamics of the ATPase complex on proteasome using its free-energy landscape. Fang R, Lu Y. STAR Protoc 4 102182 (2023)
  28. Stepping up protein degradation. Maupin-Furlow JA. Proc Natl Acad Sci U S A 116 350-352 (2019)


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