What drives the translocation of proteins?
- 1 May 1992
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 89 (9), 3770-3774
- https://doi.org/10.1073/pnas.89.9.3770
Abstract
We propose that protein translocation across membranes is driven by biased random thermal motion. This "Brownian ratchet" mechanism depends on chemical asymmetries between the cis and trans sides of the membrane. Several mechanisms could contribute to rectifying the thermal motion of the protein, such as binding and dissociation of chaperonins to the translocating chain, chain coiling induced by pH and/or ionic gradients, glycosylation, and disulfide bond formation. This helps explain the robustness and promiscuity of these transport systems.Keywords
This publication has 36 references indexed in Scilit:
- Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences.Journal of Biological Chemistry, 1991
- Ras C-terminal processing enzymes—New drug targets?Cell, 1991
- Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteinsNature, 1990
- The Structure and Insertion of Integral Proteins in MembranesAnnual Review of Cell Biology, 1990
- Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria.Journal of Biological Chemistry, 1990
- Protein motors and Maxwell's demons: Does mechanochemical transduction involve a thermal ratchet?Advances in Biophysics, 1990
- Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.1989
- Chemical factors that influence nucleocytoplasmic transport: a fluorescence photobleaching study.The Journal of cell biology, 1986
- Determinants for protein localization: beta-lactamase signal sequence directs globin across microsomal membranes.Proceedings of the National Academy of Sciences of the United States of America, 1984
- Coupled cell-free synthesis, segregation, and core glycosylation of a secretory proteinProceedings of the National Academy of Sciences of the United States of America, 1978