Cargando…
Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp
The transportation of membrane proteins through the aqueous subcellular space is an important and challenging process. Its molecular mechanism and the associated structural change are poorly understood. Periplasmic chaperones, such as Skp in Escherichia coli, play key roles in the transportation and...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458824/ https://www.ncbi.nlm.nih.gov/pubmed/23049938 http://dx.doi.org/10.1371/journal.pone.0046068 |
_version_ | 1782244709915164672 |
---|---|
author | Lyu, Zhi-Xin Shao, Qiang Gao, Yi Qin Zhao, Xin Sheng |
author_facet | Lyu, Zhi-Xin Shao, Qiang Gao, Yi Qin Zhao, Xin Sheng |
author_sort | Lyu, Zhi-Xin |
collection | PubMed |
description | The transportation of membrane proteins through the aqueous subcellular space is an important and challenging process. Its molecular mechanism and the associated structural change are poorly understood. Periplasmic chaperones, such as Skp in Escherichia coli, play key roles in the transportation and protection of outer membrane proteins (OMPs) in Gram-negative bacteria. The molecular mechanism through which Skp interacts with and protects OMPs remains mysterious. Here, a combined experimental and molecular dynamics simulation study was performed to gain the structural and dynamical information in the process of OMPs and Skp binding. Stopped-flow experiments on site specific mutated and labeled Skp and several OMPs, namely OmpC, the transmembrane domain of OmpA, and OmpF, allowed us to obtain the mechanism of OMP entering the Skp cavity, and molecular dynamics simulations yielded detailed molecular interactions responsible for this process. Both experiment and simulation show that the entrance of OMP into Skp is a highly directional process, which is initiated by the interaction between the N-terminus of OMP and the bottom “tentacle” domain of Skp. The opening of the more flexible tentacle of Skp, the non-specific electrostatic interactions between OMP and Skp, and the constant formation and breaking of salt bridges between Skp and its substrate together allow OMP to enter Skp and gradually “climb” into the Skp cavity in the absence of an external energy supply. |
format | Online Article Text |
id | pubmed-3458824 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34588242012-10-03 Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp Lyu, Zhi-Xin Shao, Qiang Gao, Yi Qin Zhao, Xin Sheng PLoS One Research Article The transportation of membrane proteins through the aqueous subcellular space is an important and challenging process. Its molecular mechanism and the associated structural change are poorly understood. Periplasmic chaperones, such as Skp in Escherichia coli, play key roles in the transportation and protection of outer membrane proteins (OMPs) in Gram-negative bacteria. The molecular mechanism through which Skp interacts with and protects OMPs remains mysterious. Here, a combined experimental and molecular dynamics simulation study was performed to gain the structural and dynamical information in the process of OMPs and Skp binding. Stopped-flow experiments on site specific mutated and labeled Skp and several OMPs, namely OmpC, the transmembrane domain of OmpA, and OmpF, allowed us to obtain the mechanism of OMP entering the Skp cavity, and molecular dynamics simulations yielded detailed molecular interactions responsible for this process. Both experiment and simulation show that the entrance of OMP into Skp is a highly directional process, which is initiated by the interaction between the N-terminus of OMP and the bottom “tentacle” domain of Skp. The opening of the more flexible tentacle of Skp, the non-specific electrostatic interactions between OMP and Skp, and the constant formation and breaking of salt bridges between Skp and its substrate together allow OMP to enter Skp and gradually “climb” into the Skp cavity in the absence of an external energy supply. Public Library of Science 2012-09-26 /pmc/articles/PMC3458824/ /pubmed/23049938 http://dx.doi.org/10.1371/journal.pone.0046068 Text en © 2012 Lyu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Lyu, Zhi-Xin Shao, Qiang Gao, Yi Qin Zhao, Xin Sheng Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title | Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title_full | Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title_fullStr | Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title_full_unstemmed | Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title_short | Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp |
title_sort | direct observation of the uptake of outer membrane proteins by the periplasmic chaperone skp |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458824/ https://www.ncbi.nlm.nih.gov/pubmed/23049938 http://dx.doi.org/10.1371/journal.pone.0046068 |
work_keys_str_mv | AT lyuzhixin directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT shaoqiang directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT gaoyiqin directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT zhaoxinsheng directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp |