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• W2906475661 abstract "Cryoelectron microscopy (cryo-EM) has revolutionized knowledge of protein remodeling and unfolding by ATPases of the AAA (ATPases associated with various cellular activities) family, including those associated with energy-dependent proteolysis. A study in PNAS by Majumder et al. (1) provides insight into evolutionary conserved functions of AAA-ATPases through cryo-EM single-particle analysis of the archaeal AAA-ATPase proteasome-activating nucleotidase (PAN) bound to 20S proteasomes [core particles (CPs)]. Five conformational states of PAN were identified in the presence of adenosine 5′-O-(3-thiotriphosphate) (ATPγS) that now guide understanding of its functional cycle in the conversion of nucleotide binding, hydrolysis, and release into the gripping, unfolding, and translocation of substrate proteins into the proteasomal CP for destruction. Particularly striking is the sequential cycle of the PAN ATPase that relies on nucleotide-dependent intersubunit signaling to trigger residues to grip and move substrate protein through its central pore. The mechanism can be described as protomers traversing down a spiral staircase of substrate engagement; the step from the bottom to the top provides the protomer its next turn in the sequential ATPase cycle that is interwoven with substrate engagement and unfolding. This around-the-ring ATP cycle is observed for related ATPases of the AAA+ superfamily of eukaryotes and bacteria that unfold proteins, revealing that the mechanism is ancient and conserved in all domains of life.Proteasomes are energy-dependent proteases needed for proteostasis and the regulated turnover of proteins associated with metabolism, signaling, cell cycle control, stress responses, and other important cellular processes (2). Proteasomes are widespread and essential for survival of eukaryotes (3) and archaea (4) and are needed for the persistence of mycobacteria (5). This central function provides impetus for the design and … [↵][1]1Email: jmaupin{at}ufl.edu. [1]: #xref-corresp-1-1" @default.
• W2906475661 created "2019-01-01" @default.
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• W2906475661 date "2018-12-19" @default.
• W2906475661 modified "2023-10-16" @default.
• W2906475661 title "Stepping up protein degradation" @default.
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• W2906475661 doi "https://doi.org/10.1073/pnas.1819949116" @default.
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