Optimal Efficiency of ClpAP and ClpXP Chaperone-Proteases Is Achieved by Architectural Symmetry (CROSBI ID 244985)
Prilog u časopisu | izvorni znanstveni rad
Podaci o odgovornosti
Maglica, Željka ; Kolygo, Kristina ; Weber-Ban, Eilika
engleski
Optimal Efficiency of ClpAP and ClpXP Chaperone-Proteases Is Achieved by Architectural Symmetry
A common feature of chaperone-proteases is architectural two-fold symmetry across the proteolytic cylinder. Here we investigate the role of symmetry for the function of ClpAP and ClpXP assemblies. We generated asymmetric ClpP particles in which the two rings differ in ClpA and ClpX binding capability and/or in proteolytic activity. Rapid-kinetic fluorescence measurements and steady-state experiments indicate that single 2:1 ClpAP or ClpXP complexes are as efficient in substrate degradation as two 1:1 ClpAP or ClpXP assemblies. This implies that the two chaperone components work independently. However, an asymmetric ClpP particle composed of one active and one inactive ring can stimulate ATPase activity of ClpA regardless of whether ClpA binds to the active ring or to the opposite side of ClpP, across the ring of inactivated protease. Thus, we propose that conformational transitions in ClpP are concerted and allosteric effects are transferred simultaneously to both associated chaperones, leading to synchronized activation.
ATP-dependent protease ; Endopeptidase ClpP ; ClpAP ; ClpXP ; AAA ATPase ; Degradation
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o izdanju
Povezanost rada
Biologija, Interdisciplinarne prirodne znanosti, Kemija