Bacterial type II toxin-antitoxin systems acting through post-translational modifications
The post-translational modification (PTM) serves as an important molecular switch mechanism to modulate diverse biological functions in response to specific cues. Though more commonly found in eukaryotic cells, many PTMs have been identified and characterized in bacteria over the past decade, highli...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-01-01
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| Series: | Computational and Structural Biotechnology Journal |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037020305274 |
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| author | Si-Ping Zhang Han-Zhong Feng Qian Wang Megan L. Kempher Shuo-Wei Quan Xuanyu Tao Shaomin Niu Yong Wang Hu-Yuan Feng Yong-Xing He |
| author_facet | Si-Ping Zhang Han-Zhong Feng Qian Wang Megan L. Kempher Shuo-Wei Quan Xuanyu Tao Shaomin Niu Yong Wang Hu-Yuan Feng Yong-Xing He |
| author_sort | Si-Ping Zhang |
| collection | DOAJ |
| description | The post-translational modification (PTM) serves as an important molecular switch mechanism to modulate diverse biological functions in response to specific cues. Though more commonly found in eukaryotic cells, many PTMs have been identified and characterized in bacteria over the past decade, highlighting the importance of PTMs in regulating bacterial physiology. Several bacterial PTM enzymes have been characterized to function as the toxin component of type II TA systems, which consist of a toxin that inhibits cell growth and an antitoxin that protects the cell from poisoning by the toxin. While TA systems can be classified into seven types based on nature of the antitoxin and its activity, type II TA systems are perhaps the most studied among the different TA types and widely distributed in eubacteria and archaea. The type II toxins possessing PTM activities typically modify various cellular targets mostly associated with protein translation and DNA replication. This review mainly focuses on the enzymatic activities, target specificities, antitoxin neutralizing mechanisms of the different families of PTM toxins. We also proposed that TA systems can be conceptually viewed as molecular switches where the ‘on’ and ‘off’ state of the system is tightly controlled by antitoxins and discussed the perspective on toxins having other physiologically roles apart from growth inhibition by acting on the nonessential cellular targets. |
| first_indexed | 2024-12-20T17:01:29Z |
| format | Article |
| id | doaj.art-9234664b9bbf442c9255aa7ab614fca1 |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-12-20T17:01:29Z |
| publishDate | 2021-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-9234664b9bbf442c9255aa7ab614fca12022-12-21T19:32:30ZengElsevierComputational and Structural Biotechnology Journal2001-03702021-01-01198693Bacterial type II toxin-antitoxin systems acting through post-translational modificationsSi-Ping Zhang0Han-Zhong Feng1Qian Wang2Megan L. Kempher3Shuo-Wei Quan4Xuanyu Tao5Shaomin Niu6Yong Wang7Hu-Yuan Feng8Yong-Xing He9Ministry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR ChinaMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR ChinaMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR ChinaInstitute for Environmental Genomics, Department of Microbiology and Plant Biology, University of Oklahoma, Norman, OK, USAMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR ChinaInstitute for Environmental Genomics, Department of Microbiology and Plant Biology, University of Oklahoma, Norman, OK, USAInstitute of Urology, Lanzhou University Second Hospital, Key Laboratory of Urological Diseases in Gansu Province, Gansu Nephro-Urological Clinical Center, Lanzhou, PR ChinaMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR ChinaMinistry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR China; Corresponding authors.Ministry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, PR China; Corresponding authors.The post-translational modification (PTM) serves as an important molecular switch mechanism to modulate diverse biological functions in response to specific cues. Though more commonly found in eukaryotic cells, many PTMs have been identified and characterized in bacteria over the past decade, highlighting the importance of PTMs in regulating bacterial physiology. Several bacterial PTM enzymes have been characterized to function as the toxin component of type II TA systems, which consist of a toxin that inhibits cell growth and an antitoxin that protects the cell from poisoning by the toxin. While TA systems can be classified into seven types based on nature of the antitoxin and its activity, type II TA systems are perhaps the most studied among the different TA types and widely distributed in eubacteria and archaea. The type II toxins possessing PTM activities typically modify various cellular targets mostly associated with protein translation and DNA replication. This review mainly focuses on the enzymatic activities, target specificities, antitoxin neutralizing mechanisms of the different families of PTM toxins. We also proposed that TA systems can be conceptually viewed as molecular switches where the ‘on’ and ‘off’ state of the system is tightly controlled by antitoxins and discussed the perspective on toxins having other physiologically roles apart from growth inhibition by acting on the nonessential cellular targets.http://www.sciencedirect.com/science/article/pii/S2001037020305274TA systemPhosphorylationAMPylationADP-ribosylationAcetylationPersistence |
| spellingShingle | Si-Ping Zhang Han-Zhong Feng Qian Wang Megan L. Kempher Shuo-Wei Quan Xuanyu Tao Shaomin Niu Yong Wang Hu-Yuan Feng Yong-Xing He Bacterial type II toxin-antitoxin systems acting through post-translational modifications Computational and Structural Biotechnology Journal TA system Phosphorylation AMPylation ADP-ribosylation Acetylation Persistence |
| title | Bacterial type II toxin-antitoxin systems acting through post-translational modifications |
| title_full | Bacterial type II toxin-antitoxin systems acting through post-translational modifications |
| title_fullStr | Bacterial type II toxin-antitoxin systems acting through post-translational modifications |
| title_full_unstemmed | Bacterial type II toxin-antitoxin systems acting through post-translational modifications |
| title_short | Bacterial type II toxin-antitoxin systems acting through post-translational modifications |
| title_sort | bacterial type ii toxin antitoxin systems acting through post translational modifications |
| topic | TA system Phosphorylation AMPylation ADP-ribosylation Acetylation Persistence |
| url | http://www.sciencedirect.com/science/article/pii/S2001037020305274 |
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