ATP‐dependent protein refolding activity in reticulocyte lysate
- 27 September 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 331 (1-2) , 25-30
- https://doi.org/10.1016/0014-5793(93)80290-b
Abstract
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 molecular weight complexes overlapping the distributions of Hsc70, Hsp90 and the chaperonin TRiC on gel filtration columns. The readdition of unfractionated cytosol and Mg-ATP was required for the efficient folding of these forms of luciferase to the active enzyme. We conclude that protein folding in the eukaryotic cytosol depends on the functional cooperation of different chaperone activities and cofactors in a complex, ATP-dependent process.Keywords
This publication has 22 references indexed in Scilit:
- The translation machinery and 70 kd heat shock protein cooperate in protein synthesisCell, 1992
- The emergence of the chaperone machinesTrends in Biochemical Sciences, 1992
- TCP1 complex is a molecular chaperone in tubulin biogenesisNature, 1992
- A cytoplasmic chaperonin that catalyzes β-actin foldingPublished by Elsevier ,1992
- Raising the roofNature, 1992
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- Protein folding in the cellNature, 1992
- THE MITOCHONDRIAL PROTEIN IMPORT APPARATUSAnnual Review of Biochemistry, 1990
- Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and AssemblyScience, 1990
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970