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- 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
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Abstract
- 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.
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Citations
Citations to this article as recorded by
- 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
- Focused Overview of Mycobacterium tuberculosis VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
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