The thermosome: alternating alpha and beta-subunits within the chaperonin of the archaeon Thermoplasma acidophilum.
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta, which are arranged in two stacked, eight-membered rings. Electron cryo-microscopy in conjunction with image analysis revealed a 4-fold symmetry in the heterooligomeric alpha + beta thermosome isolated from Thermoplasma, but not in the homooligomeric alpha-only thermosome expressed in Escherichia coli. This indicates that alpha and beta-subunits alternate within the rings of the Thermoplasma thermosome rather than forming two different homooligomeric rings. In addition, a small subpopulation of 9-fold symmetric complexes was found among the recombinant alpha-only thermosomes, and a central mass most likely representing bound substrate molecules was observed in about half of the native and recombinant thermosome particles.
Nitsch
M
M
Abt. für Molekulare Strukturbiologie, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Klumpp
M
M
Lupas
A
A
Baumeister
W
W
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D018833:Chaperonins / Q000737:chemistry*; D007053:Ice; D008854:Microscopy, Electron / Q000379:methods; D013822:Thermoplasma / Q000737:chemistry* / Q000201:enzymology / Q000648:ultrastructure
D007053:Ice; D000251:Adenosine Triphosphatases; D018833:Chaperonins