Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Anat L. Bonshtien"'
Autor:
Rajach Sharkia, Adina Niv, Anat L. Bonshtien, Itzhak Mizrahi, Celeste Weiss, Avital Parnas, Abdussalam Azem
Publikováno v:
Cell Stress and Chaperones. 14:509-519
In this study, we have investigated the relationship between chaperonin/co-chaperonin binding, ATP hydrolysis, and protein refolding in heterologous chaperonin systems from bacteria, chloroplast, and mitochondria. We characterized two types of chloro
Publikováno v:
Journal of Biological Chemistry. 282:4463-4469
Chaperonins cpn60 and cpn10 are essential proteins involved in cellular protein folding. Plant chloroplasts contain a unique version of the cpn10 co-chaperonin, cpn20, which consists of two homologous cpn10-like domains (N-cpn20 and C-cpn20) that are
Publikováno v:
Plant molecular biology. 69(3)
The chloroplast cpn20 protein is a functional homolog of the cpn10 co-chaperonin, but its gene consists of two cpn10-like units joined head-to-tail by a short chain of amino acids. This double protein is unique to plastids and was shown to exist in p
Autor:
Celeste Weiss, Itzhak Mizrahi, Paul V. Viitanen, Abdussalam Azem, Ariel Lustig, Anat L. Bonshtien, Rajach Sharkia, Adina Niv
Publikováno v:
Biochimica et biophysica acta. 1651(1-2)
Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts. Eubacteria and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperon