Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP
Open Access
- 27 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 336 (2) , 363-367
- https://doi.org/10.1016/0014-5793(93)80838-l
Abstract
Similar to chaperonins from other sources, intact chaperonin from Escherichia coli (GroEL) exists as a tetradecamer, and the ability to promote folding of other proteins has been considered to be dependent on this oligomeric structure. However, the peptide fragments of GroEL of molecular size 34–50 kDa, which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer, retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL/GroES/ATP system. This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP.Keywords
This publication has 28 references indexed in Scilit:
- A chaperonin protein module involved in recognition of interactive protein surfaces?Trends in Biochemical Sciences, 1993
- The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- Structure of holo‐chaperonin studied with electron microscopy Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes eachFEBS Letters, 1992
- Role of accessory proteins in protein folding: Current Opinion in Structural Biology 1992, 2:26…-34Current Opinion in Structural Biology, 1992
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- High molecular weight pea leaf protein similar to the groE protein of escherichia coliBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Isolation and characterization of the host protein groE involved in bacteriophage lambda assemblyJournal of Molecular Biology, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970