The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism
Type II toxin–antitoxin (TA) systems encode two proteins: a toxin that inhibits cell growth and an antitoxin that neutralizes the toxin by direct intermolecular protein–protein interactions. The bacterial HipBA TA system is implicated in persister formation. The Haemophilus influenzae HipBA TA syste...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2022-09-01
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| Series: | IUCrJ |
| Subjects: | |
| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S205225252200687X |
| _version_ | 1811183910510395392 |
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| author | Ji Sung Koo Sung-Min Kang Won-Min Jung Do-Hee Kim Bong-Jin Lee |
| author_facet | Ji Sung Koo Sung-Min Kang Won-Min Jung Do-Hee Kim Bong-Jin Lee |
| author_sort | Ji Sung Koo |
| collection | DOAJ |
| description | Type II toxin–antitoxin (TA) systems encode two proteins: a toxin that inhibits cell growth and an antitoxin that neutralizes the toxin by direct intermolecular protein–protein interactions. The bacterial HipBA TA system is implicated in persister formation. The Haemophilus influenzae HipBA TA system consists of a HipB antitoxin and a HipA toxin, the latter of which is split into two fragments, and here we investigate this novel three-component regulatory HipBA system. Structural and functional analysis revealed that HipAN corresponds to the N-terminal part of HipA from other bacteria and toxic HipAC is inactivated by HipAN, not HipB. This study will be helpful in understanding the detailed regulatory mechanism of the HipBAN+C system, as well as why it is constructed as a three-component system. |
| first_indexed | 2024-04-11T13:04:46Z |
| format | Article |
| id | doaj.art-2fa84b6bbcc44a869793f417bd5b5433 |
| institution | Directory Open Access Journal |
| issn | 2052-2525 |
| language | English |
| last_indexed | 2024-04-11T13:04:46Z |
| publishDate | 2022-09-01 |
| publisher | International Union of Crystallography |
| record_format | Article |
| series | IUCrJ |
| spelling | doaj.art-2fa84b6bbcc44a869793f417bd5b54332022-12-22T04:22:47ZengInternational Union of CrystallographyIUCrJ2052-25252022-09-019562563110.1107/S205225252200687Xlz5057The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanismJi Sung Koo0Sung-Min Kang1Won-Min Jung2Do-Hee Kim3Bong-Jin Lee4Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of KoreaCollege of Pharmacy, Duksung Women's University, Seoul 01369, Republic of KoreaResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of KoreaJeju Research Institute of Pharmaceutical Sciences, College of Pharmacy, Jeju National University, Jeju 63243, Republic of KoreaResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of KoreaType II toxin–antitoxin (TA) systems encode two proteins: a toxin that inhibits cell growth and an antitoxin that neutralizes the toxin by direct intermolecular protein–protein interactions. The bacterial HipBA TA system is implicated in persister formation. The Haemophilus influenzae HipBA TA system consists of a HipB antitoxin and a HipA toxin, the latter of which is split into two fragments, and here we investigate this novel three-component regulatory HipBA system. Structural and functional analysis revealed that HipAN corresponds to the N-terminal part of HipA from other bacteria and toxic HipAC is inactivated by HipAN, not HipB. This study will be helpful in understanding the detailed regulatory mechanism of the HipBAN+C system, as well as why it is constructed as a three-component system.http://scripts.iucr.org/cgi-bin/paper?S205225252200687Xhipbahaemophilus influenzaetoxin–antitoxin systempersister formationx-ray crystallography |
| spellingShingle | Ji Sung Koo Sung-Min Kang Won-Min Jung Do-Hee Kim Bong-Jin Lee The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism IUCrJ hipba haemophilus influenzae toxin–antitoxin system persister formation x-ray crystallography |
| title | The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism |
| title_full | The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism |
| title_fullStr | The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism |
| title_full_unstemmed | The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism |
| title_short | The Haemophilus influenzae HipBA toxin–antitoxin system adopts an unusual three-component regulatory mechanism |
| title_sort | haemophilus influenzae hipba toxin antitoxin system adopts an unusual three component regulatory mechanism |
| topic | hipba haemophilus influenzae toxin–antitoxin system persister formation x-ray crystallography |
| url | http://scripts.iucr.org/cgi-bin/paper?S205225252200687X |
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