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...

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Autores principales:	Zhi-Xin Lyu, Qiang Shao, Yi Qin Gao, Xin Sheng Zhao
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3600f87e4e694b8f8a0b6b091d2e6f2d
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spelling	oai:doaj.org-article:3600f87e4e694b8f8a0b6b091d2e6f2d2021-11-18T08:13:51ZDirect observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.1932-620310.1371/journal.pone.0046068https://doaj.org/article/3600f87e4e694b8f8a0b6b091d2e6f2d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23049938/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Zhi-Xin LyuQiang ShaoYi Qin GaoXin Sheng ZhaoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 9, p e46068 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Zhi-Xin Lyu Qiang Shao Yi Qin Gao Xin Sheng Zhao Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.
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	article
author	Zhi-Xin Lyu Qiang Shao Yi Qin Gao Xin Sheng Zhao
author_facet	Zhi-Xin Lyu Qiang Shao Yi Qin Gao Xin Sheng Zhao
author_sort	Zhi-Xin Lyu
title	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_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_sort	direct observation of the uptake of outer membrane proteins by the periplasmic chaperone skp.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/3600f87e4e694b8f8a0b6b091d2e6f2d
work_keys_str_mv	AT zhixinlyu directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT qiangshao directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT yiqingao directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp AT xinshengzhao directobservationoftheuptakeofoutermembraneproteinsbytheperiplasmicchaperoneskp
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Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.

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