- The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner
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Han Byeol Lee , Si Hyoung Park , Chang-Ro Lee
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J. Microbiol. 2021;59(7):666-674. Published online May 15, 2021
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DOI: https://doi.org/10.1007/s12275-021-1130-8
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The inner membrane protein lipopolysaccharide assembly
protein B (LapB) is an adaptor protein that activates the proteolysis
of LpxC by an essential inner membrane metalloprotease,
FtsH, leading to a decrease in the level of lipopolysaccharide
in the membrane. In this study, we revealed the
mechanism by which the essential inner membrane protein
YejM regulates LapB and analyzed the role of the transmembrane
domain of LapB in Escherichia coli. The transmembrane
domain of YejM genetically and physically interacted with
LapB and inhibited its function, which led to the accumulation
of LpxC. The transmembrane domain of LapB was indispensable
for both its physical interaction with YejM and
its regulation of LpxC proteolysis. Notably, we found that the
lapB mutant exhibited strong cold sensitivity and this phenotype
was not associated with increased accumulation of LpxC.
The transmembrane domain of LapB was also required for
its role in adaptation to cold stress. Taken together, these
results
showed that LapB plays an important role in both
the regulation of LpxC level, which is controlled by its interaction
with the transmembrane domain of YejM, and adaptation
to cold stress, which is independent of LpxC.
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Citations
Citations to this article as recorded by  - Bile and short-chain fatty acid salts affect survival and virulence of Klebsiella Oxytoca of mussel origin
Jingjing Xu, Meng Sun, Jiangcheng Chang, Qingchao Xie, Yongjie Wang, Lanming Chen
Archives of Microbiology.2025;[Epub] CrossRef - Inhibition of cardiolipin biosynthesis partially suppresses the sensitivity of an Escherichia coli mutant lacking OmpC to envelope stress
Dae-Beom Ryu, Umji Choi, Gyubin Han, Chang-Ro Lee
Journal of Microbiology.2025; 63(11): e2507004. CrossRef -
PhoPQ-mediated lipopolysaccharide modification governs intrinsic resistance to tetracycline and glycylcycline antibiotics in
Escherichia coli
Byoung Jun Choi, Umji Choi, Dae-Beom Ryu, Chang-Ro Lee, Mehrad Hamidian, You-Hee Cho
mSystems.2024;[Epub] CrossRef -
Lytic transglycosylase repertoire diversity enables intrinsic antibiotic resistance and daughter cell separation in
Escherichia coli
under acidic stress
Ji Eun Son, Si Hyoung Park, Umji Choi, Chang-Ro Lee, Laurent Poirel
Antimicrobial Agents and Chemotherapy.2024;[Epub] CrossRef - Trans-cinnamaldehyde inhibits Escherichia coli growth by regulating lipopolysaccharide accumulation
Huanling Xing, Xiaomin Liu, Jianhao Lin, Mingfei Sun, Junyi Huang, Xinghai Li, Yanqun Li, Shining Guo, Fang Zhou, Hong Wu
Food Bioscience.2024; 61: 104559. CrossRef - Coordinated and Distinct Roles of Peptidoglycan Carboxypeptidases DacC and DacA in Cell Growth and Shape Maintenance under Stress Conditions
Umji Choi, Si Hyoung Park, Han Byeol Lee, Ji Eun Son, Chang-Ro Lee, Cristina Solano
Microbiology Spectrum.2023;[Epub] CrossRef - NoiD, a DedA membrane protein required for homeostasis maintaining of Rhizobium leguminosarum biovar viciae during symbiosis with Pisum sativum
Xiaofang Li, Jiaming Xu, Yajuan Wei, Zirui Chen
Symbiosis.2022; 86(1): 81. CrossRef - Conserved Tandem Arginines for PbgA/YejM Allow Salmonella Typhimurium To Regulate LpxC and Control Lipopolysaccharide Biogenesis during Infection
Nicole P. Giordano, Joshua A. Mettlach, Zachary D. Dalebroux, Manuela Raffatellu
Infection and Immunity.2022;[Epub] CrossRef - Divergent Effects of Peptidoglycan Carboxypeptidase DacA on Intrinsic β-Lactam and Vancomycin Resistance
Si Hyoung Park, Umji Choi, Su-Hyun Ryu, Han Byeol Lee, Jin-Won Lee, Chang-Ro Lee, Krisztina M. Papp-Wallace
Microbiology Spectrum.2022;[Epub] CrossRef - Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state
Wu Liu, Martien Schoonen, Tong Wang, Sean McSweeney, Qun Liu
Communications Biology.2022;[Epub] CrossRef - Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality in Escherichia coli
Gracjana Klein, Alicja Wieczorek, Martyna Szuster, Satish Raina
International Journal of Molecular Sciences.2021; 23(1): 189. CrossRef
- Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli
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Chul Gi Sung , Umji Choi , Chang-Ro Lee
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J. Microbiol. 2020;58(7):598-605. Published online April 22, 2020
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DOI: https://doi.org/10.1007/s12275-020-0078-4
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367
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Although bacteria have diverse membrane proteins, the function
of many of them remains unknown or uncertain even
in Escherichia coli. In this study, to investigate the function
of hypothetical membrane proteins, genome-wide analysis
of phenotypes of hypothetical membrane proteins was performed
under various envelope stresses. Several genes responsible
for adaptation to envelope stresses were identified.
Among them, deletion of YhcB, a conserved inner membrane
protein of unknown function, caused high sensitivities to various
envelope stresses and increased membrane permeability,
and caused growth defect under normal growth conditions.
Furthermore, yhcB deletion resulted in morphological
aberration, such as branched shape, and cell division defects,
such as filamentous growth and the generation of chromosome-
less cells. The analysis of antibiotic susceptibility
showed that the yhcB mutant was highly susceptible to various
anti-folate antibiotics. Notably, all phenotypes of the yhcB
mutant were completely or significantly restored by YhcB
without the transmembrane domain, indicating that the localization
of YhcB on the inner membrane is dispensable for its
function. Taken together, our results demonstrate that YhcB
is involved in cell morphology and cell division in a membrane
localization-independent manner.
-
Citations
Citations to this article as recorded by - Inhibition of cardiolipin biosynthesis partially suppresses the sensitivity of an Escherichia coli mutant lacking OmpC to envelope stress
Dae-Beom Ryu, Umji Choi, Gyubin Han, Chang-Ro Lee
Journal of Microbiology.2025; 63(11): e2507004. CrossRef - Co-ordinated assembly of the multilayered cell envelope of Gram-negative bacteria
Elayne M Fivenson, Laurent Dubois, Thomas G Bernhardt
Current Opinion in Microbiology.2024; 79: 102479. CrossRef - Loss of YhcB results in overactive fatty acid biosynthesis
Hannah M. Stanley, M. Stephen Trent, K. Heran Darwin
mBio.2024;[Epub] CrossRef - A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking
Alicja Wieczorek, Anna Sendobra, Akshey Maniyeri, Magdalena Sugalska, Gracjana Klein, Satish Raina
International Journal of Molecular Sciences.2022; 23(17): 9706. CrossRef - Loss of YhcB results in dysregulation of coordinated peptidoglycan, LPS and phospholipid synthesis during Escherichia coli cell growth
Emily C. A. Goodall, Georgia L. Isom, Jessica L. Rooke, Karthik Pullela, Christopher Icke, Zihao Yang, Gabriela Boelter, Alun Jones, Isabel Warner, Rochelle Da Costa, Bing Zhang, James Rae, Wee Boon Tan, Matthias Winkle, Antoine Delhaye, Eva Heinz, Jean-F
PLOS Genetics.2021; 17(12): e1009586. CrossRef - The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner
Han Byeol Lee, Si Hyoung Park, Chang-Ro Lee
Journal of Microbiology.2021; 59(7): 666. CrossRef
- [PROTOCOL] Determination of protein phosphorylation by polyacrylamide gel electrophoresis
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Chang-Ro Lee , Young-Ha Park , Huitae Min , Yeon-Ran Kim , Yeong-Jae Seok
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J. Microbiol. 2019;57(2):93-100. Published online January 31, 2019
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DOI: https://doi.org/10.1007/s12275-019-9021-y
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327
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Abstract
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Phosphorylation is the most important modification for protein
regulation; it controls many signal transduction pathways
in all organisms. While several tools to detect phosphorylated
proteins have been developed to study a variety
of basic cellular processes involving protein phosphorylation,
these methods have several limitations. Many proteins
exhibit a phosphorylation-dependent electrophoretic mobility
shift (PDEMS) in sodium dodecyl sulfate-polyacrylamide
gel electrophoresis (SDS-PAGE), and the molecular mechanism
responsible for this phenomenon has been elucidated
recently. The method for detecting phosphorylated proteins
can be simplified by the application of the PDEMS. Herein,
we present a novel simple method to detect protein phosphorylation,
which is based on the construction of a variant
protein displaying a PDEMS. The PDEMS of proteins is
caused by the distribution of negatively charged amino acids
around the phosphorylation site, i.e. an electrophoretic mobility
shift (EMS)-related motif (ΘX1-3ΘX1-3Θ, where Θ corresponds
to an acidic or phosphorylated amino acid and X
represents any amino acid). The EMS-related motif can be
constructed by the introduction of a negative charge by phosphorylation;
it results in the decreased binding of SDS to
the proteins, consequently inducing the retardation of the
mobility of the protein during SDS-PAGE. Based on these
molecular analyses of the PDEMS, a protein with the EMSrelated
motif is designed and used to determine the in vivo
phosphorylation state of the protein. This method may be
used as a general strategy to easily measure the ratio of protein
phosphorylation in cells.
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Toxicology Letters.2021; 349: 40. CrossRef - The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner
Han Byeol Lee, Si Hyoung Park, Chang-Ro Lee
Journal of Microbiology.2021; 59(7): 666. CrossRef - Subsynaptic Distribution, Lipid Raft Targeting and G Protein-Dependent Signalling of the Type 1 Cannabinoid Receptor in Synaptosomes from the Mouse Hippocampus and Frontal Cortex
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- Molecular characterization of SCO0765 as a cellotriose releasing endo-β-1,4-cellulase from Streptomyces coelicolor A(3)
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Joo-Bin Hong , Vijayalakshmi Dhakshnamoorthy , Chang-Ro Lee
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J. Microbiol. 2016;54(9):626-631. Published online August 31, 2016
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DOI: https://doi.org/10.1007/s12275-016-6271-9
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341
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Abstract
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The sco0765 gene was annotated as a glycosyl hydrolase family
5 endoglucanase from the genomic sequence of Streptomyces
coelicolor A3(2) and consisted of 2,241 bp encoding a
polypeptide of 747 amino acids (molecular weight of 80.5
kDa) with a 29-amino acid signal peptide for secretion. The
SCO0765 recombinant protein was heterogeneously overexpressed
in Streptomyces lividans TK24 under the control
of a strong ermE* promoter. The purified SCO0765 protein
showed the expected molecular weight of the mature form
(718 aa, 77.6 kDa) on sodium dodecyl sulfate-polyacryl amide
gel electrophoresis. SCO0765 showed high activity toward
β-glucan and carboxymethyl cellulose (CMC) and negligible
activity to Avicel, xylan, and xyloglucan. The SCO0765 cellulase
had a maximum activity at pH 6.0 and 40°C toward
CMC and at pH 9.0 and 50–60°C toward β-glucan. Thin
layer chromatography of the hydrolyzed products of CMC
and β-glucan by SCO0765 gave cellotriose as the major product
and cellotetraose, cellopentaose, and longer oligosaccharides
as the minor products. These results clearly demonstrate
that SCO0765 is an endo-β-1,4-cellulase, hydrolyzing
the β-1,4 glycosidic bond of cellulose into cellotriose.
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