Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES Journal Article

  

Authors:	Martin, J.; Geromanos, S.; Tempst, P.; Hartl, F. U.
Article Title:	Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES
Abstract:	THE chaperonin GroEL, a tetradecameric cylinder consisting of subunits of Mr∼60,000 (60K), and its cofactor GroES, a heptameric ring of 10K subunits, mediate protein folding in the cytosol of Escherichia coll 1ĝ€"3. In the presence of nucleotide, GroES forms a 1:1 complex with GroEL which binds unfolded protein in its central cavity and releases it to allow folding upon ATP hydrolysis 4ĝ€"7. Using labelling with azido-ATP, we have identified a protease-stable nucleotide-binding domain of Mr 40K in the GroEL subunits (residues 153-531). Azido-ATP is crosslinked to the highly conserved Tyr 477, indicating that this residue is close to the purine ring of the bound nucleotide. Surprisingly, GroES also binds ATP cooperatively and with an affinity comparable to that of GroEL. Azido-nucleotide labelling of GroES subunits occurs at the conserved Tyr 71 in a protease-stable 6.5K domain (starting at residue 33). Proteinase K cleavage at residue 32 is prevented when GroES is bound to GroEL. ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP to facilitate cooperative ATP binding and hydrolysis for substrate protein release. © 1993 Nature Publishing Group.
Keywords:	nonhuman; tyrosine; bacterial proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; escherichia coli; binding site; binding sites; adenosine triphosphate; protein folding; ligand binding; nucleotides; heat-shock proteins; escherichia; adenosine triphosphate derivative; priority journal; article; support, non-u.s. gov't; chaperonin; groel protein; groes protein
Journal Title:	Nature
Volume:	366
Issue:	6452
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Date Published:	1993-11-18
Start Page:	279
End Page:	282
Language:	English
DOI:	10.1038/366279a0
PUBMED:	7901771
PROVIDER:	scopus
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027427329&doi=10.1038%2f366279a0&partnerID=40&md5=81da31d7e541d8946b636fe4bbcbd065
Notes:	Article -- Export Date: 1 March 2019 -- Source: Scopus

https://synapse.mskcc.org/synapse/works/has_related_data_chk/144279