- Functional characterization of HigBA toxin-antitoxin system in an Arctic bacterium, Bosea sp. PAMC 26642
-
Eunsil Choi , Ahhyun Huh , Changmin Oh , Jeong-Il Oh , Ho Young Kang , Jihwan Hwang
-
J. Microbiol. 2022;60(2):192-206. Published online February 1, 2022
-
DOI: https://doi.org/10.1007/s12275-022-1619-9
-
-
951
View
-
3
Download
-
3
Web of Science
-
3
Crossref
-
Abstract
PDF
-
Toxin-antitoxin (TA) systems are growth-controlling genetic
elements consisting of an intracellular toxin protein and its
cognate antitoxin. TA systems have been spread among microbial
genomes through horizontal gene transfer and are
now prevalent in most bacterial and archaeal genomes. Under
normal growth conditions, antitoxins tightly counteract the
activity of the toxins. Upon stresses, antitoxins are inactivated,
releasing activated toxins, which induce growth arrest or cell
death. In this study, among nine functional TA modules in
Bosea sp. PAMC 26642 living in Arctic lichen, we investigated
the functionality of BoHigBA2. BohigBA2 is located close to
a genomic island and adjacent to flagellar gene clusters. The
expression of BohigB2 induced the inhibition of E. coli growth
at 37°C, which was more manifest at 18°C, and this growth
defect was reversed when BohigA2 was co-expressed, suggesting
that this BoHigBA2 module might be an active TA
module in Bosea sp. PAMC 26642. Live/dead staining and
viable count analyses revealed that the BoHigB2 toxin had
a bactericidal effect, causing cell death. Furthermore, we demonstrated
that BoHigB2 possessed mRNA-specific ribonuclease
activity on various mRNAs and cleaved only mRNAs
being translated, which might impede overall translation and
consequently lead to cell death. Our study provides the insight
to understand the cold adaptation of Bosea sp. PAMC 26642
living in the Arctic.
-
Citations
Citations to this article as recorded by 
- Evaluating the Contribution of the Predicted Toxin–Antitoxin System HigBA to Persistence, Biofilm Formation, and Virulence in Burkholderia pseudomallei
Itziar Chapartegui-González, Nittaya Khakhum, Jacob L. Stockton, Alfredo G. Torres, Igor E. Brodsky Infection and Immunity.2022;[Epub] CrossRef - Chronicle of Research into Lichen-Associated Bacteria
Zichen He, Takeshi Naganuma Microorganisms.2022; 10(11): 2111. CrossRef - Degradation of amoxicillin by newly isolated Bosea sp. Ads-6
Lei Yan, Ning Yan, Xi-Yan Gao, Ying Liu, Zhi-Pei Liu Science of The Total Environment.2022; 828: 154411. CrossRef
- Functional and structural characterization of Deinococcus radiodurans R1 MazEF toxin-antitoxin system, Dr0416-Dr0417
-
Immanuel Dhanasingh , Eunsil Choi , Jeongeun Lee , Sung Haeng Lee , Jihwan Hwang
-
J. Microbiol. 2021;59(2):186-201. Published online February 1, 2021
-
DOI: https://doi.org/10.1007/s12275-021-0523-z
-
-
965
View
-
5
Download
-
6
Web of Science
-
4
Crossref
-
Abstract
PDF
-
In prokaryotes, toxin-antitoxin (TA) systems are commonly
found. They likely reflect the adaptation of pathogenic bacteria
or extremophiles to various unfavorable environments
by slowing their growth rate. Genomic analysis of the extremophile
Deinococcus radiodurans R1 revealed the presence of
eight type II TA systems, including the genes dr0417, dr0660,
dr1530, dr0690, and dr1807. Expression of these toxin genes
led to inhibition of Escherichia coli growth, whereas their
antidote antitoxins were able to recover the growth defect.
Remarkably, Dr0417 (DrMazF) showed endoribonuclease activity
toward rRNAs as well as mRNAs, as determined by in
vivo and in vitro RNA cleavage assays, and this activity was
inhibited by Dr0416 (DrMazE). It was also found that the expression
of dr0416-0417 module is directly regulated by the
DrMazE-MazF complex. Furthermore, this TA module was
induced under stress conditions and plays an important role
in survival. To understand the regulatory mechanism at the
molecular level, we determined the first high-resolution structures
of DrMazF alone and of the DrMazE-MazF complex.
In contrast with the hetero-hexameric state of typical MazEMazF
complexes found in other species, DrMazE-MazF crystal
structure consists of a hetero-trimer, with the DNA-binding
domain of DrMazE undergoing self-cleavage at the flexible
linker loop. Our structure revealed that the unique residue
R54 provides an additional positive charge to the substratebinding
pocket of DrMazF, its mutation significantly affects
the endonuclease activity. Thus, our work reports the unique
structural and biochemical features of the DrMazE-MazF
system.
-
Citations
Citations to this article as recorded by 
- SeaMoon: From protein language models to continuous structural heterogeneity
Valentin Lombard, Dan Timsit, Sergei Grudinin, Elodie Laine Structure.2025; 33(9): 1577. CrossRef - Focused Overview of Mycobacterium tuberculosis VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
Sung-Min Kang Biomimetics.2023; 8(5): 412. CrossRef - Functional characterization of HigBA toxin-antitoxin system in an Arctic bacterium, Bosea sp. PAMC 26642
Eunsil Choi, Ahhyun Huh, Changmin Oh, Jeong-Il Oh, Ho Young Kang, Jihwan Hwang Journal of Microbiology.2022; 60(2): 192. CrossRef - Identification and characterization of the type II toxin-antitoxin systems in the carbapenem-resistant Acinetobacter baumannii
Alireza Japoni-Nejad, Elnaz Harifi Mood, Parastoo Ehsani, Soroush Sardari, Fatemah Sadeghpour Heravi, Saeid Bouzari, Nader Shahrokhi Microbial Pathogenesis.2021; 158: 105052. CrossRef
- Functional analysis of Vibrio vulnificus RND efflux pumps homologous to Vibrio cholerae VexAB and VexCD, and to Escherichia coli AcrAB
-
Seunghwa Lee , Ji-Hyun Yeom , Sojin Seo , Minho Lee , Sarang Kim , Jeehyeon Bae , Kangseok Lee , Jihwan Hwang
-
J. Microbiol. 2015;53(4):256-261. Published online March 4, 2015
-
DOI: https://doi.org/10.1007/s12275-015-5037-0
-
-
1,045
View
-
0
Download
-
11
Crossref
-
Abstract
PDF
-
Resistance-nodulation-division (RND) efflux pumps are associated
with multidrug resistance in many gram-negative
pathogens. The genome of Vibrio vulnificus encodes 11 putative
RND pumps homologous to those of Vibrio cholerae
and Escherichia coli. In this study, we analyzed three putative
RND efflux pumps, showing homology to V. cholerae VexAB
and VexCD and to E. coli AcrAB, for their functional roles in
multidrug resistance of V. vulnificus. Deletion of the vexAB
homolog resulted in increased susceptibility of V. vulnificus
to bile acid, acriflavine, ethidium bromide, and erythromycin,
whereas deletion of acrAB homologs rendered V. vulnificus
more susceptible to acriflavine only. Deletion of vexCD had
no effect on susceptibility of V. vulnificus to these chemicals.
Upon exposure to these antibacterial chemicals, expression
of tolCV1 and tolCV2, which are putative outer membrane
factors of RND efflux pumps, was induced, whereas expression
levels of vexAB, vexCD, and acrAB homologs were not
significantly changed. Our results show that the V. vulnificus
homologs of VexAB largely contributed to in vitro antimicrobial
resistance with a broad substrate specificity that
was partially redundant with the AcrAB pump homologs.
-
Citations
Citations to this article as recorded by 
- Bile compounds are effective inducer of efflux pump-mediated antimicrobial resistance among Gram-negative bacteria
Hanieh Akbari, Robab Azargun, Mina Yekani, Somayeh Ahmadi, Hadi Ghanbari, Mohammad Yousef Memar, Tahereh Pirzadeh Biologia.2025; 80(6): 1443. CrossRef - Functions and Regulation of the Outer Membrane Protein TolC in Vibrio Species
Yue Gong, Chunxia Liu, Xin Tian, Young Ran Kim ACS Infectious Diseases.2025; 11(7): 1756. CrossRef - Dynamics of efflux pumps in antimicrobial resistance, persistence, and community living of Vibrionaceae
Sanath Kumar, Manjusha Lekshmi, Jerusha Stephen, Anely Ortiz-Alegria, Matthew Ayitah, Manuel F. Varela Archives of Microbiology.2024;[Epub] CrossRef - Membrane Efflux Pumps of Pathogenic Vibrio Species: Role in Antimicrobial Resistance and Virulence
Jerusha Stephen, Manjusha Lekshmi, Parvathi Ammini, Sanath H. Kumar, Manuel F. Varela Microorganisms.2022; 10(2): 382. CrossRef - TolCV1 Has Multifaceted Roles During Vibrio vulnificus Infection
Yue Gong, Rui Hong Guo, Joon Haeng Rhee, Young Ran Kim Frontiers in Cellular and Infection Microbiology.2021;[Epub] CrossRef - The mechanisms that regulate Vibrio parahaemolyticus virulence gene expression differ between pathotypes
Nicholas Petronella, Jennifer Ronholm
Microbial Genomics
.2018;[Epub] CrossRef - ATP-Binding Cassette Transporter VcaM from Vibrio cholerae is Dependent on the Outer Membrane Factor Family for Its Function
Wen-Jung Lu, Hsuan-Ju Lin, Thamarai Janganan, Cheng-Yi Li, Wei-Chiang Chin, Vassiliy Bavro, Hong-Ting Lin International Journal of Molecular Sciences.2018; 19(4): 1000. CrossRef - Contribution of efflux systems to the detergent resistance, cytotoxicity, and biofilm formation of Vibrio vulnificus
Chung-Cheng Lo, Pei-Ting Lin, Chuan Chiang-Ni, Kuan-Hua Lin, Shin-Luen Lee, Tzu-Fang Kuo, Horng-Ren Lo Gene Reports.2017; 9: 115. CrossRef - Survival of the Fittest: How Bacterial Pathogens Utilize Bile To Enhance Infection
Jeticia R. Sistrunk, Kourtney P. Nickerson, Rachael B. Chanin, David A. Rasko, Christina S. Faherty Clinical Microbiology Reviews.2016; 29(4): 819. CrossRef - MdsABC-Mediated Pathway for Pathogenicity in Salmonella enterica Serovar Typhimurium
Saemee Song, Boeun Lee, Ji-Hyun Yeom, Soonhye Hwang, Ilnam Kang, Jang-Cheon Cho, Nam-Chul Ha, Jeehyeon Bae, Kangseok Lee, Yong-Hak Kim, S. M. Payne Infection and Immunity.2015; 83(11): 4266. 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 Journal of Microbiology.2015; 53(6): 355. CrossRef
|