PDZ-like domains mediate binding specificity in the Clp/Hsp 100 family of chaperones and protease regulatory subunits

Article Abstract:

The molecular chaperone ClpX consists of tandem modular domains binding to the C-terminal sequences of target proteins in a way that parallels functional specificity. Such C-terminal sequences are shown as disordered peptides on the surface of proteins. Conservation of ClpX binding domains shows that the route of substrate recognition characterized for ClpX would be a conserved feature in Clp/Hsp 100 family members.

Observations, Protein binding, Cell research, Cytological research

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Asymmetric interactions of ATP with the AAA+ ClpX(sub 6) unfoldase: Allosteric control of a protein machine

Article Abstract:

The commonalities between distant AAA+ family members, including protein and DNA translocases, helicases, motor proteins, clamp loaders, and other ATP-dependent enzymes are studied. Concentrated hydrolysis models involving ClpX(sub 6).ATP(sub 6) or ClpX(sub 6).ADP(sub 6) are rules out and the structures of hexameric AAA+ machines with three or four nucleotides are highlighted as likely functional states.

Science & research, Biological Product (except Diagnostic) Manufacturing, Drugs, Deoxyribonucleic Acid, Nucleic Acid Derivatives, Research, DNA, Nucleotides

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Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA(sup)+ degradation machine

Article Abstract:

Research indicates that during protein processing, the ATP turnover rate is 4-fold slower during denaturation than translocation. However, total ATP consumption increases with substrate stability and destabilization of substrate structure accelerate degradation with concomittant reduction in ATP consumption.

United States, Usage, Physiological aspects, Protein folding, Protein structure, Protein denaturation

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