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Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.

<div class='caption-title'>(A) Surface-representation side view of the HslUV protease (PDB: 5JI3).</div>
<div class='caption-title'>(A) Class-average negative-stain electron microscopy (EM) images of WTHslU (top row) compared with projections of a plugged hexamer (PDB: 6PXK) filtered to 15-Å resolution (bottom row). Samples were prepared at room temperature.</div>
<div class='caption-title'>(A) Model for activation of HslU by thermal melting of the autoinhibitory plug.</div>
Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT
OpenAccess logo Cell Rep 34 108639 (2021)
Related entries: 6pxi, 6pxl

Cited: 8 times
EuropePMC logo PMID: 33472065

Abstract

At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU6 unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV12 peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis.

Articles - 6pxk mentioned but not cited (2)

  1. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT. Cell Rep 34 108639 (2021)
  2. Molecular characterization of a tetra segmented ssDNA virus infecting Botrytis cinerea worldwide. Ruiz-Padilla A, Turina M, Ayllón MA. Virol J 20 306 (2023)


Reviews citing this publication (3)

  1. Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria. Izert MA, Klimecka MM, Górna MW. Front Mol Biosci 8 669762 (2021)
  2. Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality in Escherichia coli. Klein G, Wieczorek A, Szuster M, Raina S. Int J Mol Sci 23 189 (2021)
  3. Targeting bacterial degradation machinery as an antibacterial strategy. Petkov R, Camp AH, Isaacson RL, Torpey JH. Biochem J 480 1719-1731 (2023)

Articles citing this publication (3)

  1. A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Ghanbarpour A, Cohen SE, Fei X, Kinman LF, Bell TA, Zhang JJ, Baker TA, Davis JH, Sauer RT. Nat Commun 14 7281 (2023)
  2. A Transient π-π or Cation-π Interaction between Degron and Degrader Dual Residues: A Key Step for the Substrate Recognition and Discrimination in the Processive Degradation of SulA by ClpYQ (HslUV) Protease in Escherichia coli. Lin CH, Tsai CH, Chou CC, Wu WF. Int J Mol Sci 24 17353 (2023)
  3. Conformational variability of cyanobacterial ChlI, the AAA+ motor of magnesium chelatase involved in chlorophyll biosynthesis. Shvarev D, Scholz AI, Moeller A. mBio 14 e0189323 (2023)


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