title: Effects of the inter-ring communication in GroEL structural and functional asymmetry.
abstract: The chaperonin GroEL consists of a double-ring structure that assists protein folding in the presence of GroES and ATP. Recent studies suggest that the 7-mer ring is the functional unit where protein folding takes place. Nevertheless, both GroEL rings are required to complete the reaction cycle through signals transmitted between the two rings. Electron microscopy, image processing, and biochemical analysis of GroEL, a single-ring mutant (SR1) and a inter-ring communication affected mutant (A126V), in the presence of ATP and adenylyl imidodiphosphate, have allowed the identification of a conformational change in the apical domains that is strictly dependent on the communication between the two GroEL rings. It is deduced from these results that the binding of nucleotide to both GroEL rings generates, as a consequence of the inter-ring communication, a functionally and structurally asymmetric particle. This asymmetric particle has a ring with a small conformational change in its apical domains and high affinity toward unfolded substrate and GroES, and the other ring has a larger conformational change in its apical domains and lower affinity toward substrate and GroES.
authors.affiliation: Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas, Campus Universidad Autónoma de Madrid, 28049 Madrid, Spain.
authors.forename: O
authors.initials: O
authors.lastname: Llorca
authors.forename: J
authors.initials: J
authors.lastname: Pérez-Pérez
authors.forename: J L
authors.initials: JL
authors.lastname: Carrascosa
authors.forename: A
authors.initials: A
authors.lastname: Galán
authors.forename: A
authors.initials: A
authors.lastname: Muga
authors.forename: J M
authors.initials: JM
authors.lastname: Valpuesta
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D000818:Animals; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D008291:Malate Dehydrogenase / Q000378:metabolism; D008854:Microscopy, Electron; D017354:Point Mutation; D011188:Potassium / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D013552:Swine; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D008291:Malate Dehydrogenase; D013884:Thiosulfate Sulfurtransferase; D011188:Potassium