S. Diamant et al., INCREASED EFFICIENCY OF GROE-ASSISTED PROTEIN-FOLDING BY MANGANESE IONS, The Journal of biological chemistry, 270(47), 1995, pp. 28387-28391
This study addresses the role of ATP-bound and free Mg2+ and Mn2+ ions
in the activation and modulation of chaperonin-assisted refolding of
urea-denatured malate dehydrogenase. As compared with Mg2+, Mn2+ ions
caused a significant increase in the rate of GroE-assisted malate dehy
drogenase refolding and, concomitantly, a decrease in the rate of ATP
hydrolysis. Moreover, Mn2+ increases the affinity of GroES for GroEL,
even in the presence of saturating amounts of Mg2+ Chemical cross-link
ing showed that lower concentrations of Mn-ATP as compared with Mg-ATP
are needed to form both asymmetric GroEL(14)GroES(7) and symmetric Gr
oEL(14)(GroES(7))(2) particles. The manganese-dependent increase in th
e rate of protein folding concurred with a specific increase in the am
ount of symmetric GroEL(14)-(GroES(7))(2) particles detected in a chap
eronin solution. Thus, Mn2+ is a cofactor that can markedly increase t
he efficiency of the chaperonin reaction in vitro, Mn2+ ions can serve
as an important tool for analyzing the molecular mechanism and the st
ructure of chaperonins.