Go-expression of the two genes encoding the alpha- and beta-subunit of the Thermoplasma acidophilum thermosome in Escher ichia coli yielded fully assembled hetero-oligomeric complexes (alpha + beta). Surprisingly, also separate expression of both genes resulted in formation of hexadecameric complexes (alpha, beta) in the bacterial cytoplasm. On electron micrographs these complexes were indistinguishable from each other and from the native thermosome. The recombinant alpha-complex as well as the native thermosome could be reconstituted in vitro from their dissociated subunits in the presence of Mg-ATP. [References: 28
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
Chaperonins are multi-subunit double-ring complexed composed of 60-kDa proteins that are believed to...
In this study we describe, the construction of a co-expression vector allowing simultaneous producti...
Go-expression of the two genes encoding the alpha- and beta-subunit of the Thermoplasma acidophilum ...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta,...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
A high molecular-mass protein complex from the archaebacterium Thermoplasma acidophilum, referred to...
The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains ...
Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformat...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
The purification and characterization of a new type of thermostable chaperonin from the archaebacter...
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subu...
Protein folding by chaperonins is powered by ATP binding and hydrolysis. ATPase activity drives the ...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
Chaperonins are multi-subunit double-ring complexed composed of 60-kDa proteins that are believed to...
In this study we describe, the construction of a co-expression vector allowing simultaneous producti...
Go-expression of the two genes encoding the alpha- and beta-subunit of the Thermoplasma acidophilum ...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta,...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
A high molecular-mass protein complex from the archaebacterium Thermoplasma acidophilum, referred to...
The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains ...
Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformat...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
The purification and characterization of a new type of thermostable chaperonin from the archaebacter...
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subu...
Protein folding by chaperonins is powered by ATP binding and hydrolysis. ATPase activity drives the ...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
Chaperonins are multi-subunit double-ring complexed composed of 60-kDa proteins that are believed to...
In this study we describe, the construction of a co-expression vector allowing simultaneous producti...