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Posttranslational quality control: folding, refolding, and degrading proteins.
Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over proteinExpand
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RcsA, an unstable positive regulator of capsular polysaccharide synthesis.
RcsA is an unstable positive regulator required for the synthesis of colanic acid capsular polysaccharide in Escherichia coli. Degradation of the RcsA protein in vivo depends on the ATP-dependent LonExpand
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ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
The ATP-dependent Clp protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic active site, and ClpA, which possesses ATPase activity and activates theExpand
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The RssB response regulator directly targets sigma(S) for degradation by ClpXP.
The sigma(S) subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. Control over sigma(S) activity is exercised in part by regulatedExpand
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A molecular chaperone, ClpA, functions like DnaK and DnaJ.
The two major molecular chaperone families that mediate ATP-dependent protein folding and refolding are the heat shock proteins Hsp60s (GroEL) and Hsp70s (DnaK). Clp proteins, like chaperones, areExpand
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Crystal Structure of ClpA, an Hsp100 Chaperone and Regulator of ClpAP Protease*
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation ofExpand
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Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.
The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp PExpand
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Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
In ClpXP and ClpAP complexes, ClpA and ClpX use the energy of ATP hydrolysis to unfold proteins and translocate them into the self-compartmentalized ClpP protease. ClpP requires the ATPases toExpand
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Protein quality control: triage by chaperones and proteases.
Proteases and chaperones together serve to maintain quahty control of cellular proteins. Both types of en­ zymes have as their substrates the variety of misfolded and partially folded proteins thatExpand
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Regulation by proteolysis: energy-dependent proteases and their targets.
A number of critical regulatory proteins in both prokaryotic and eukaryotic cells are subject to rapid, energy-dependent proteolysis. Rapid degradation combined with control over biosynthesisExpand
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