| Structure of phosphorylated-like RssB, the adaptor delivering sigma[s] to the ClpXP proteolytic machinery, reveals an interface switch for activation. | Structure of phosphorylated-like RssB, the adaptor delivering σ(s) to the ClpXP proteolytic machinery, reveals an interface switch for activation.
Brugger C, Schwartz J, Novick S, Tong S, Hoskins JR, Majdalani N, Kim R, Filipovski M, Wickner S, Gottesman S, Griffin PR, Deaconescu AM., Free PMC Article | 01/31/2024 |
| Degradation of MinD oscillator complexes by Escherichia coli ClpXP. | Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
LaBreck CJ, Trebino CE, Ferreira CN, Morrison JJ, DiBiasio EC, Conti J, Camberg JL., Free PMC Article | 08/28/2021 |
| A split protease-E. coli ClpXP system quantifies protein-protein interactions in Escherichia coli cells. | A split protease-E. coli ClpXP system quantifies protein-protein interactions in Escherichia coli cells.
Wang S, Zhang F, Mei M, Wang T, Yun Y, Yang S, Zhang G, Yi L., Free PMC Article | 08/21/2021 |
| Results indicate that hinge-linker length and flexibility are optimized for efficient substrate unfolding and support a model in which the hinge-linker elements of ClpX facilitate efficient degradation both by maintaining proper ring geometry and facilitating subunit-subunit communication. | Hinge-Linker Elements in the AAA+ Protein Unfoldase ClpX Mediate Intersubunit Communication, Assembly, and Mechanical Activity.
Bell TA, Baker TA, Sauer RT., Free PMC Article | 07/20/2019 |
| When the weak C-tag signal is replaced with a The AAA + unfoldase ClpX specifically recognizes two classes of recognition tags in the MuA transposase,specific features of these MuA tag classes direct ClpX to the biologically important reaction path. | Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.
Ling L, Montaño SP, Sauer RT, Rice PA, Baker TA., Free PMC Article | 12/5/2015 |
| Antirestriction activity of the mercury resistance nonconjugative transposon Tn5053 is controlled by the protease ClpXP | [Antirestriction activity of the mercury resistance nonconjugative transposon Tn5053 is controlled by the protease ClpXP].
Zavigel'skiĭ GB, Kotova VIu, Mel'kina OE, Pustovoĭt KS. | 03/28/2015 |
| When ClpX encounters a folded protein, it either overcomes this mechanical barrier or slips on the polypeptide before making another unfolding attempt. Binding of ClpP decreases the slip probability and enhances the unfolding efficiency of ClpX. | ClpX(P) generates mechanical force to unfold and translocate its protein substrates.
Maillard RA, Chistol G, Sen M, Righini M, Tan J, Kaiser CM, Hodges C, Martin A, Bustamante C., Free PMC Article | 07/2/2011 |
| Together, our results suggested that ClpXP modulates cell division through degradation of FtsZ and possibly other cell division components that function downstream of FtsZ ring assembly. | The interplay of ClpXP with the cell division machinery in Escherichia coli.
Camberg JL, Hoskins JR, Wickner S., Free PMC Article | 06/18/2011 |
| results also reveal highly conserved residues in the ClpX-binding peptides of both E. coli SspB and C. crescentus SspBalpha that play no detectable role in ClpX-binding or substrate delivery. | Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species.
Chowdhury T, Chien P, Ebrahim S, Sauer RT, Baker TA., Free PMC Article | 03/22/2010 |
| The crystal structures presented here reveal striking asymmetry in ring hexamers of nucleotide-free and nucleotide-bound ClpX. | Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| Results suggest that ClpXP may participate in cell division by modulating the equilibrium between free and polymeric FtsZ via degradation of FtsZ filaments and protomers. | ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics.
Camberg JL, Hoskins JR, Wickner S., Free PMC Article | 01/21/2010 |
| analysis of ClpXP adaptors and substrates | Engineering synthetic adaptors and substrates for controlled ClpXP degradation.
Davis JH, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| ClpXP degrades UvrA at different rates during the distinct stages of post-UV recovery when the cells contain different levels of unrepaired cyclobutane pyrimidine dimers. | Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage.
Pruteanu M, Baker TA., Free PMC Article | 01/21/2010 |
| Loss of clpP and clpX genes leads to a moderate fourfold increase in spontaneous mutagenesis. | Spontaneous mutagenesis is elevated in protease-defective cells.
Al Mamun AA, Humayun MZ. | 01/21/2010 |
| Results show that a tyrosine residue in a pore loop of the hexameric ClpX unfoldase links ATP hydrolysis to mechanical work by gripping substrates during unfolding and translocation. | Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.
Martin A, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| ClpXP, together with SspB, is uniquely adapted for degradation of SsrA-tagged proteins and is responsible for the major part of their degradation in vivo | Turnover of endogenous SsrA-tagged proteins mediated by ATP-dependent proteases in Escherichia coli.
Lies M, Maurizi MR., Free PMC Article | 01/21/2010 |
| Results reveal that the ssrA tag interacts with different loops that form the top, middle, and lower portions of the central channel of the ClpX hexamer. | Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.
Martin A, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| Results describe how substrate multimerization modulates recognition by the ClpX unfoldase using a natural substrate, MuA transposase. | Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX.
Abdelhakim AH, Oakes EC, Sauer RT, Baker TA., Free PMC Article | 01/21/2010 |
| The results support a model in which ClpX unfolding of GFP progresses via a metastable intermediate, which must be captured by several fast ATP-dependent translocation steps to prevent the protein from refolding and therefore escaping degradation. | Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes.
Martin A, Baker TA, Sauer RT. | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.
Wojtkowiak D, Georgopoulos C, Zylicz M. | 11/5/2007 |
| These results support a major role for the RKH loops in substrate recognition and suggest that ClpX specificity represents an evolutionary compromise that has optimized degradation of multiple types of substrates rather than any single class. | Altered specificity of a AAA+ protease.
Farrell CM, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| the binding site of the ClpX dimeric cofactor, SspB2, on the zinc-binding domain (ZBD) in ClpX was determined by NMR and mutational analysis | Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX.
Thibault G, Yudin J, Wong P, Tsitrin V, Sprangers R, Zhao R, Houry WA., Free PMC Article | 01/21/2010 |
| degradation of T. thermophilus RNase-H by ClpX supports a model in which ClpX denatures proteins by initially unfolding structural elements attached to the degradation tag, and correlates well with the mapping of local protein stability | Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation.
Kenniston JA, Burton RE, Siddiqui SM, Baker TA, Sauer RT. | 01/21/2010 |
| Discrete static and dynamic interactions mediate binding and communication between ClpX and ClpP. | Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.
Martin A, Baker TA, Sauer RT., Free PMC Article | 01/21/2010 |
| data suggest that ClpAP and ClpXP may recognize and bind substrates in significantly different ways | Binding and degradation of heterodimeric substrates by ClpAP and ClpXP.
Sharma S, Hoskins JR, Wickner S. | 01/21/2010 |