doi: 10.1038/348339a0.
(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
Affiliations
- PMID: 1979147
- DOI: 10.1038/348339a0
Item in Clipboard
(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
Nature.
.
Abstract
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 improper protein structures or aggregates. As GroEL is isolated and functions as a 20-25S tetradecameric particle (GroELp), the question arises--what is the mechanism of its own assembly? Here we show the (Mg-ATP)-dependent self-stimulation ('self-chaperoning') in vitro of GroELp reassembly from its monomeric state.
Similar articles
-
A simple and rapid method for the purification of GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins.Protein Expr Purif. 1993 Dec;4(6):580-4. doi: 10.1006/prep.1993.1076. Protein Expr Purif. 1993. PMID: 7904492
-
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.Nature. 1993 Nov 18;366(6452):228-33. doi: 10.1038/366228a0. Nature. 1993. PMID: 7901770
-
Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE.J Mol Biol. 2001 Feb 2;305(5):1173-83. doi: 10.1006/jmbi.2000.4373. J Mol Biol. 2001. PMID: 11162122
-
The chaperonin cycle and protein folding.Bioessays. 1994 Apr;16(4):229-31. doi: 10.1002/bies.950160404. Bioessays. 1994. PMID: 7913317 Review.
-
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):313-25; discussion 325-6. doi: 10.1098/rstb.1993.0030. Philos Trans R Soc Lond B Biol Sci. 1993. PMID: 8098536 Review.
Cited by
-
Molecular chaperones and protein folding in plants.Plant Mol Biol. 1996 Oct;32(1-2):191-222. doi: 10.1007/BF00039383. Plant Mol Biol. 1996. PMID: 8980480 Review.
-
Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Protein Expr Purif. 2018 Feb;142:8-15. doi: 10.1016/j.pep.2017.09.010. Epub 2017 Sep 22. Protein Expr Purif. 2018. PMID: 28951283 Free PMC article.
-
Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering.Protein Sci. 2003 Apr;12(4):672-80. doi: 10.1110/ps.0233603. Protein Sci. 2003. PMID: 12649424 Free PMC article.
-
Atomic force microscopy visualizes ATP-dependent dissociation of multimeric TATA-binding protein before translocation into the cell nucleus.Pflugers Arch. 1996 Sep;432(5):839-44. doi: 10.1007/s004240050206. Pflugers Arch. 1996. PMID: 8772134
-
In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties.Molecules. 2023 Feb 16;28(4):1901. doi: 10.3390/molecules28041901. Molecules. 2023. PMID: 36838891 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
