Characterization of Homo-oligomeric Complexes of α and β Chaperonin Subunits from the Acidothermophilic Archaeon,Sulfolobussp. Strain 7
Authors:
- Masafumi YohdaMasafumi Yohda
- Makoto SuzukiMSMakoto Suzuki
- Kazumori YazakiKYKazumori Yazaki
- Kin-Ichiro MiuraKMKin-Ichiro Miura
- Isao EndoIEIsao Endo
- 26 January 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 242 (3) , 640-647
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro‐complexesThe EMBO Journal, 1997
- GroEL‐Mediated protein foldingProtein Science, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- Expression of an archaeal chaperonin in E. coli: formation of homo‐ (α, β) and hetero‐oligomeric (α + β) thermosome complexesFEBS Letters, 1995
- Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groesCell, 1995
- The Chaperonin Containing t-complex polypeptide 1 (TCP-1). Multisubunit Machinery Assisting in Protein Folding and Assembly in the Eukaryotic CytosolEuropean Journal of Biochemistry, 1995
- The Thermosome of Thermoplasma acidophilum and Its Relationship to the Eukaryotic Chaperonin TRiCEuropean Journal of Biochemistry, 1995
- Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domainsTrends in Biochemical Sciences, 1994
- Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopyNature, 1994
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988