Type I chaperonins: not all are created equal

FEBS Letters

Ben-Tal, Nir¹  Azem, Abdussalam¹  Bell, Rachel E¹  Levy-Rimler, Galit¹ 

[1] Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69778, Israel

关键词: Chaperonin;    cpn60;    cpn10;    GroEL;    GroES;    Type I chaperonin;   

DOI  :  10.1016/S0014-5793(02)03178-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. Since their discovery, the bacterial chaperonins have provided an excellent model system for investigating the mechanism by which chaperonins mediate protein folding. Due to the high conservation of the primary sequence among Type I chaperonins, it is generally accepted that organellar chaperonins function similar to the bacterial ones. However, recent studies indicate that the chloroplast and mitochondrial chaperonins possess unique structural and functional properties that distinguish them from their bacterial homologs. This review focuses on the unique properties of organellar chaperonins.

【 授权许可】

Unknown