Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae.
The major heat shock proteins in the archaeon Sulfolobus shibatae are similar to the cytosolic eukaryotic chaperonin and form an 18-subunit bitoroidal complex. Two sequence-related subunits constitute a functional complex, named the archaeosome. The archaeosome exists in two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure. The equilibrium between the complexes and free subunits is affected by ATP and temperature. Denatured proteins associate with both conformational states as well as with free subunits that form an intermediate complex. These unexpected observations suggest a new mechanism of archaeosome-mediated thermotolerance and protein folding.
D000255:Adenosine Triphosphate / Q000378:metabolism; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D008854:Microscopy, Electron; D018832:Molecular Chaperones / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D016944:Sulfolobus / Q000737:chemistry*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins