Academic Journal
Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria.
العنوان: | Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria. |
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المؤلفون: | Michael C Chao, Karen J Kieser, Shoko Minami, Daniela Mavrici, Bree B Aldridge, Sarah M Fortune, Tom Alber, Eric J Rubin |
المصدر: | PLoS Pathogens, Vol 9, Iss 2, p e1003197 (2013) |
بيانات النشر: | Public Library of Science (PLoS), 2013. |
سنة النشر: | 2013 |
المجموعة: | LCC:Immunologic diseases. Allergy LCC:Biology (General) |
مصطلحات موضوعية: | Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5 |
الوصف: | Peptidoglycan hydrolases are a double-edged sword. They are required for normal cell division, but when dysregulated can become autolysins lethal to bacteria. How bacteria ensure that peptidoglycan hydrolases function only in the correct spatial and temporal context remains largely unknown. Here, we demonstrate that dysregulation converts the essential mycobacterial peptidoglycan hydrolase RipA to an autolysin that compromises cellular structural integrity. We find that mycobacteria control RipA activity through two interconnected levels of regulation in vivo-protein interactions coordinate PG hydrolysis, while proteolysis is necessary for RipA enzymatic activity. Dysregulation of RipA protein complexes by treatment with a peptidoglycan synthase inhibitor leads to excessive RipA activity and impairment of correct morphology. Furthermore, expression of a RipA dominant negative mutant or of differentially processed RipA homologues reveals that RipA is produced as a zymogen, requiring proteolytic processing for activity. The amount of RipA processing differs between fast-growing and slow-growing mycobacteria and correlates with the requirement for peptidoglycan hydrolase activity in these species. Together, the complex picture of RipA regulation is a part of a growing paradigm for careful control of cell wall hydrolysis by bacteria during growth, and may represent a novel target for chemotherapy development. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 1553-7366 1553-7374 |
Relation: | http://europepmc.org/articles/PMC3585148?pdf=render; https://doaj.org/toc/1553-7366; https://doaj.org/toc/1553-7374 |
DOI: | 10.1371/journal.ppat.1003197 |
URL الوصول: | https://doaj.org/article/30ff609cce2e49018fc57f5688d1a709 |
رقم الانضمام: | edsdoj.30ff609cce2e49018fc57f5688d1a709 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 15537366 15537374 |
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DOI: | 10.1371/journal.ppat.1003197 |