Chaperoning Rubisco in purple bacteria

DIONISI, H.; SUSANA KARINA CHECA; FERREYRA, R. G.; VIALE, A. M.

In Microbial Growth on C1 Compounds

Kluwer Academic Publishers

Lugar: Dordrecht; Año: 1996; p. 175 - 182

Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) has played a pivotal role in the identification of the so-called molecular chaperones (Ellis 1994; Hartman, Harpel 1994), families of highly conserved proteins present in all organisms which play fundamental roles in the assembly, transport and degradation of cellular polypeptides as well as in the protection against cell injuries from many origins (Georgopoulos, Welch 1993; Ellis 1994). The chaperonins represent a subset of molecular chaperones, ubiquitously distributed among eubacteria, chloroplasts and mitochondria (Georgopoulos, Welch 1993; Ellis 1994; Viale et al. 1994). Two distinct members (GroEL and GroES) compose this family, which are encoded by a common operon (groESL) in most bacteria (Georgopoulos, Welch 1993; Viale et al. 1994). At present, Escherichia coli (E. coli) chaperonins constitute the best characterized members of the family (Georgopoulos, Welch 1993; Ellis 1994; Hartl et al. 1994), although studies on these proteins isolated from other bacteria suggest, in principle, a common mechanism of assisted folding (Terlesky, Tabita 1991; Soncini et al. 1992; Torres-Ruiz, McFadden, 1992; Saibil et al. 1993; Ellis 1994).