V. Repka (Complex Research Institute of Viticulture and Oenology, Bratislava, Slovak Republic): Molecular chaperonins. - Biologické listy 62 (3): 193-218, 1998.

The chaperonins represent a class of sequence-related molecular chaperones originally found in all bacteria examined (including eubacteria, archebacteria, cyanobacteria, and rickettsiae), in all mitochondria examined (including those from yeast, plant and animal cells), as well as in all plastids examined to date (including chloroplasts, chromoplasts, and etioplasts). There is a high degree of sequence relatedness within the chaperonin group. The chaperonins are all abundant constitutive proteins that increase in amount after different kinds of stress such as heat shock, bacterial infection, and an increased intracellular content of unfolded proteins. There are two types of chaperonin that are sequence-related to each other. The larger type is called chaperonin 60 (cpn60), while the smaller type is called chaperonin 10 (cpn10). The bacterial and plastid chaperonin 60 oligomers respond to added ATP by hydrolyzing it and dissociating reversibly to smaller forms. Bacterial and mitochondrial chaperonin 10 bind to chaperonin 60 in the presence of MgATP and then suppresses the ATPase activity of the latter. In this review we first bring forth the concept of chaperonins and then discuss a few selected examples.