The protein folding capacity of rabbit reticulocyte cytosol was analyzed using the renaturation of firefly luciferase as a sensitive assay. In the absence of ATP, the aggregation of denatured luciferase diluted into reticulocyte lysate was prevented. Chaperone-stabilized luciferase was detected in high mo...
However, the detailed mechanisms of HOP-assisted, chaperone-dependent protein folding are largely unknown. Here, we report that HOP has ATPase activity and changes its conformation in the presence of ATP. We discuss the possible roles of ATP-dependent conformational changes in regulating HOP function...
The important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 is a typical molecular chaperone. It possesses ATPase activity and interacts in ATP-driven reactions with non-folded proteins to stimulate their correct folding and/or assembly by preventing the formation of impr...
We have developed an assay for chaperone-mediated protein renaturation using thermally denatured Firefly luciferase. Dilution of denatured luciferase (> 99% loss of activity) into reticulocyte lysate typically results in recovery of 5-15% activity. Addition of an ATP-regenerating system increases yields...
Protein FoldingWe have developed an assay for chaperone-mediated protein renaturation using thermally denatured Firefly luciferase. Dilution of denatured luciferase (> 99% loss of activity) into reticulocyte lysate typically results in recovery of 5-15% activity. Addition of an ATP-regenerating system ...
Our results demonstrate that a DExH/D-box protein has a specific, physiologically relevant chaperone function in the folding of a natural RNA substrate. 展开 关键词: tenascin lipid rafts cerebellum DOI: 10.1016/S0092-8674(02)00771-7 被引量: 278 ...
Thorough biochemical analyses revealed that ATRX cooperates with a novel H3.3-specific histone chaperone termed DAXX (death domain associated protein) [100,111,112]. Thus, to date two different ATP-dependent chromatin remodeling factors have been implicated in H3.3 incorporation...
This result suggests that the growth defect of the DnaK-deficient strain is primarily due to non-functional MetA because MetA, an inherently unstable protein even at the physiological temperature of 37°C, requires folding assistance from the DnaK chaperone system. The stabilized MetA mutants also ...
Chaperone Activity of Isolated Hybrid Chaperonins We examined the effect of hybrid chaperonins on the folding of IPMDH from T. thermophilus under a condition in which the yield of spontaneous folding was only ∼10% (Fig. 6). The following experiments were carried out in the presence of ATP....
In addition to their well-established protein-quality control function these oligomeric proteolytic complexes with chaperone-like activities may function as molecular chaperones promoting productive folding and assembly of subunit proteins. In this review, we summarize the current knowledge of the functional...