Pushing, pulling and trapping--modes of motor protein supported protein translocation |
| |
Authors: | Tomkiewicz Danuta Nouwen Nico Driessen Arnold J M |
| |
Affiliation: | Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. |
| |
Abstract: | Protein translocation across the cellular membranes is an ubiquitous and crucial activity of cells. This process is mediated by translocases that consist of a protein conducting channel and an associated motor protein. Motor proteins interact with protein substrates and utilize the free energy of ATP binding and hydrolysis for protein unfolding, translocation and unbinding. Since motor proteins are found either at the cis- or trans-side of the membrane, different mechanisms for translocation have been proposed. In the Power stroke model, cis-acting motors are thought to push, while trans-motors pull on the substrate protein during translocation. In the Brownian ratchet model, translocation occurs by diffusion of the unfolded polypeptide through the translocation pore while directionality is achieved by trapping and refolding. Recent insights in the structure and function of the molecular motors suggest that different mechanisms can be employed simultaneously. |
| |
Keywords: | CTD, small C-terminal zinc-binding domain ER, endoplasmic reticulum JDP, J-domain protein NBD, nucleotide binding domain NEF, nucleotide exchange factor PAM, presequence translocase-associated motor PBD, preprotein binding domain PCC, protein conducting channel PMF, proton motive force ΔpH, transmembrane pH gradient Δψ, transmembrane electrical potential |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|