Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.

Wojtkowiak, Diana; Georgopoulos, Costa; Żylicz, Maciej

doi:10.1016/s0021-9258(18)41572-4

Cited by 235 publications

(19 citation statements)

References 45 publications

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“…[ [26][27][28]. ClpXP's function is greatly enhanced by the presence of multiple binding sites for substrate via interaction with a molecular chaperone, SspB [29][30][31][32][33][34][35].…”

Section: Introductionmentioning

confidence: 99%

A queueing approach to multi-site enzyme kinetics

2014

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Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency ‘waiting line’ of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding sites. A natural queueing systems analogy is found to provide substantial insight into the dynamics of the model. From this, we derive exact results for the probability distribution of the enzyme configuration and for the distribution of substrate departure times in the case of identical but distinguishable classes of substrate molecules. Comments are also provided for the case when different classes of substrate molecules are not processed identically.

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“…[ [26][27][28]. ClpXP's function is greatly enhanced by the presence of multiple binding sites for substrate via interaction with a molecular chaperone, SspB [29][30][31][32][33][34][35].…”

Section: Introductionmentioning

confidence: 99%

A queueing approach to multi-site enzyme kinetics

2014

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“…Herein, we demonstrate that through a physical association with an unrelated oligo-Hsp104 functions in this process directly. Unlike other meric protease ClpP (Katayama-Fujimura et al, 1987; chaperones, Hsp104 does not prevent the aggregation Hwang et al, 1988;Wojtkowiak et al, 1993). In the abof denatured proteins.…”

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confidence: 99%

Hsp104, Hsp70, and Hsp40

Glover

Lindquist

1998

Cell

1,272

591

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Hsp104 is a stress tolerance factor that promotes the reactivation of heat-damaged proteins in yeast by an unknown mechanism. Herein, we demonstrate that Hsp104 functions in this process directly. Unlike other chaperones, Hsp104 does not prevent the aggregation of denatured proteins. However, in concert with Hsp40 and Hsp70, Hsp104 can reactivate proteins that have been denatured and allowed to aggregate, substrates refractory to the action of other chaperones. Hsp104 cooperates with the chaperones present in reticulocyte lysates but not with DnaK of E. coli. We conclude that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.

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“…The substrate specificity of ClpP thus appears to be dictated by its cooperating, physically-associated chaperone partner. Such a conclusion has been anticipated by the work of Zylicz, Georgopoulos and coworkers, who carried out a biochemical screen designed to identify proteases in E. coli lysates that could degrade the shorthalf-life protein O [8]. They uncovered a homologue of ClpA and ClpB, called ClpX, which turns out to be a 'half'-Clp, equivalent to just the carboxy-terminal homology block present in ClpA/B.…”

Section: The Clpschaperones Directing Degradationmentioning

confidence: 90%