These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60.
    Author: Levy-Rimler G, Viitanen P, Weiss C, Sharkia R, Greenberg A, Niv A, Lustig A, Delarea Y, Azem A.
    Journal: Eur J Biochem; 2001 Jun; 268(12):3465-72. PubMed ID: 11422376.
    Abstract:
    Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. The goal of this study was to investigate the structure and function of the mammalian mitochondrial chaperonin system. We present evidence that the 60 kDa chaperonin (mt-cpn60) exists in solution in dynamic equilibrium between monomers, heptameric single rings and double-ringed tetradecamers. In the presence of ATP and the 10 kDa cochaperonin (mt-cpn10), the formation of a double ring is favored. ADP at very high concentrations does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10. We propose that the cis (mt-cpn60)14.nucleotide.(mt-cpn10)7 complex is not a stable species and does not bind ADP effectively at its trans binding site.
    [Abstract] [Full Text] [Related] [New Search]