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Essential function of the N-termini tails of the proteasome for the gating mechanism revealed by molecular dynamics simulations

Ishida, Hisashi

Proteasome is involved in the degradation of proteins. Proteasome activators bind to the proteasome core particle (CP) and facilitate opening a gate of the CP, where Tyr8 and Asp9 in the N-termini tails of the CP form the ordered open gate. Four different molecular dynamics simulations were carried out: ordered- and Tyr8Gly/Asp9Gly disordered-gate models of the CP complexed with an ATP-independent PA26 and ordered- and disordered-gate models of the CP complexed with an ATP-dependent PAN-like activator. In the ordered-gate models, the substrate in the activator was more stable than that in the CP. In the disordered-gate models, the substrate in the activator was more destabilized than in the ordered-gate models. Thus, it was concluded that the dynamics of the N-termini tails entropically play a key role in the translocation of the substrate.

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Category:Biochemistry & Molecular Biology

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