- Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system
-
Inseong Jo , Jin-Sik Kim , Yongbin Xu , Jaekyung Hyun , Kangseok Lee , Nam-Chul Ha
-
J. Microbiol. 2019;57(3):185-194. Published online February 26, 2019
-
DOI: https://doi.org/10.1007/s12275-019-8520-1
-
-
980
View
-
2
Download
-
10
Web of Science
-
8
Crossref
-
 Abstract
 PDF
-
Tripartite efflux pumps and the type I secretion system of
Gram-negative bacteria are large protein complexes that span
the entire cell envelope. These complexes expel antibiotics and
other toxic substances or transport protein toxins from bacterial
cells. Elucidating the binary and ternary complex structures
at an atomic resolution are crucial to understanding the
assembly and working mechanism. Recent advances in cryoelectron
microscopy along with the construction of chimeric
proteins drastically shifted the assembly models. In this review,
we describe the current assembly models from a historical
perspective and emphasize the common assembly mechanism
for the assembly of diverse tripartite pumps and type
I secretion systems.
-
Citations
Citations to this article as recorded by  - Molecular Insights into CLD Domain Dynamics and Toxin Recruitment of the HlyA E. coli T1SS
Rocco Gentile, Stephan Schott-Verdugo, Sakshi Khosa, Cigdem Günes, Michele Bonus, Jens Reiners, Sander H.J. Smits, Lutz Schmitt, Holger Gohlke
Journal of Molecular Biology.2025; 437(24): 169485. CrossRef - Molecular mechanisms of antibiotic resistance revisited
Elizabeth M. Darby, Eleftheria Trampari, Pauline Siasat, Maria Solsona Gaya, Ilyas Alav, Mark A. Webber, Jessica M. A. Blair
Nature Reviews Microbiology.2023; 21(5): 280. CrossRef - Permeation of Fosfomycin through the Phosphate-Specific Channels OprP and OprO of Pseudomonas aeruginosa
Vinaya Kumar Golla, Claudio Piselli, Ulrich Kleinekathöfer, Roland Benz
The Journal of Physical Chemistry B.2022; 126(7): 1388. CrossRef - Adaptation of the periplasm to maintain spatial constraints essential for cell envelope processes and cell viability
Eric Mandela, Christopher J Stubenrauch, David Ryoo, Hyea Hwang, Eli J Cohen, Von L Torres, Pankaj Deo, Chaille T Webb, Cheng Huang, Ralf B Schittenhelm, Morgan Beeby, JC Gumbart, Trevor Lithgow, Iain D Hay
eLife.2022;[Epub] CrossRef - Structure, Assembly, and Function of Tripartite Efflux
and Type 1 Secretion Systems in Gram-Negative Bacteria
Ilyas Alav, Jessica Kobylka, Miriam S. Kuth, Klaas M. Pos, Martin Picard, Jessica M. A. Blair, Vassiliy N. Bavro
Chemical Reviews.2021; 121(9): 5479. CrossRef - Biotechnological applications of type 1 secretion systems
Zohreh Pourhassan N., Sander H.J. Smits, Jung Hoon Ahn, Lutz Schmitt
Biotechnology Advances.2021; 53: 107864. CrossRef - Protein-Protein Interactions in the Cytoplasmic Membrane of Escherichia coli: Influence of the Overexpression of Diverse Transporter-Encoding Genes on the Activities of PTS Sugar Uptake Systems
Mohammad Aboulwafa, Zhongge Zhang, Milton H. Saier Jr.
Microbial Physiology.2020; 30(1-6): 36. CrossRef - Perspectives towards antibiotic resistance: from molecules to population
Joon-Hee Lee
Journal of Microbiology.2019; 57(3): 181. CrossRef
- Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model
-
Saemee Song , Jin-Sik Kim , Kangseok Lee , Nam-Chul Ha
-
J. Microbiol. 2015;53(6):355-364. Published online May 30, 2015
-
DOI: https://doi.org/10.1007/s12275-015-5248-4
-
-
946
View
-
0
Download
-
9
Crossref
-
Abstract
PDF
-
Gram-negative bacteria expel a wide range of toxic substances
through tripartite drug efflux pumps consisting of an inner
membrane transporter, an outer membrane channel protein,
and a periplasmic adaptor protein. These pumps form tripartite
assemblies which can span the entire cell envelope,
including the inner and outer membranes. There have been
controversial findings regarding the assembly of the individual
components in tripartite drug efflux pumps. Recent
structural and functional studies have advanced our understanding
of the assembly and working mechanisms of the
pumps. Here, we re-evaluate the assembly models based on
recent structural and functional studies. In particular, this
study focuses on the ‘adaptor bridging model’, highlighting
the intermeshing cogwheel-like interactions between the tip
regions of the outer membrane channel protein and the periplasmic
adaptor protein in the hexameric assembly.
-
Citations
Citations to this article as recorded by - Structural Features and Energetics of the Periplasmic Entrance Opening of the Outer Membrane Channel TolC Revealed by Molecular Dynamics Simulation and Markov State Model Analysis
Jingwei Weng, Wenning Wang
Journal of Chemical Information and Modeling.2019; 59(5): 2359. CrossRef - Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system
Inseong Jo, Jin-Sik Kim, Yongbin Xu, Jaekyung Hyun, Kangseok Lee, Nam-Chul Ha
Journal of Microbiology.2019; 57(3): 185. CrossRef - Antibiotic Hybrids: the Next Generation of Agents and Adjuvants against Gram-Negative Pathogens?
Ronald Domalaon, Temilolu Idowu, George G. Zhanel, Frank Schweizer
Clinical Microbiology Reviews.2018;[Epub] CrossRef - Genetic identification of factors for extracellular cellulose accumulation in the thermophilic cyanobacterium Thermosynechococcus vulcanus: proposal of a novel tripartite secretion system
Kaisei Maeda, Jyunya Tamura, Yukiko Okuda, Rei Narikawa, Takafumi Midorikawa, Masahiko Ikeuchi
Molecular Microbiology.2018; 109(1): 121. CrossRef - Switch Loop Flexibility Affects Substrate Transport of the AcrB Efflux Pump
Reinke T. Müller, Timothy Travers, Hi-jea Cha, Joshua L. Phillips, S. Gnanakaran, Klaas M. Pos
Journal of Molecular Biology.2017; 429(24): 3863. CrossRef - Molecular Rationale behind the Differential Substrate Specificity of Bacterial RND Multi-Drug Transporters
Venkata Krishnan Ramaswamy, Attilio V. Vargiu, Giuliano Malloci, Jürg Dreier, Paolo Ruggerone
Scientific Reports.2017;[Epub] CrossRef - Structure of the MacAB–TolC ABC-type tripartite multidrug efflux pump
Anthony W. P. Fitzpatrick, Salomé Llabrés, Arthur Neuberger, James N. Blaza, Xiao-Chen Bai, Ui Okada, Satoshi Murakami, Hendrik W. van Veen, Ulrich Zachariae, Sjors H. W. Scheres, Ben F. Luisi, Dijun Du
Nature Microbiology.2017;[Epub] CrossRef - Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane Fusion Protein and Nucleotide-Binding Domain
Daichi Murata, Hiroyuki Okano, Clement Angkawidjaja, Masato Akutsu, Shun-ichi Tanaka, Kenyu Kitahara, Takuya Yoshizawa, Hiroyoshi Matsumura, Yuji Kado, Eiichi Mizohata, Tsuyoshi Inoue, Satoshi Sano, Yuichi Koga, Shigenori Kanaya, Kazufumi Takano
Biochemistry.2017; 56(47): 6281. CrossRef - The Crystal Structure of the YknZ Extracellular Domain of ABC Transporter YknWXYZ from Bacillus amyloliquefaciens
Yongbin Xu, Jianyun Guo, Lulu Wang, Rui Jiang, Xiaoling Jin, Jing Liu, Shengdi Fan, Chun-Shan Quan, Nam-Chul Ha, Bostjan Kobe
PLOS ONE.2016; 11(5): e0155846. CrossRef
|
MSK
