Cargando…
Rate-limiting transport of positively charged arginine residues through the Sec-machinery is integral to the mechanism of protein secretion
Transport of proteins across and into membranes is a fundamental biological process with the vast majority being conducted by the ubiquitous Sec machinery. In bacteria, this is usually achieved when the SecY-complex engages the cytosolic ATPase SecA (secretion) or translating ribosomes (insertion)....
Autores principales: | Allen, William J, Corey, Robin A, Watkins, Daniel W, Oliveira, A Sofia F, Hards, Kiel, Cook, Gregory M, Collinson, Ian |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9110029/ https://www.ncbi.nlm.nih.gov/pubmed/35486093 http://dx.doi.org/10.7554/eLife.77586 |
Ejemplares similares
-
ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery
por: Corey, Robin A, et al.
Publicado: (2019) -
Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation
por: Allen, William John, et al.
Publicado: (2016) -
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis
por: Alvira, Sara, et al.
Publicado: (2020) -
Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/αSNAP without HOPS
por: Song, Hongki, et al.
Publicado: (2021) -
Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering
por: Song, Hongki, et al.
Publicado: (2021)