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Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria
BACKGROUND: Sensing and responding to environmental changes is a central aspect of cell division regulation. Mycobacterium tuberculosis contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases is...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3019181/ https://www.ncbi.nlm.nih.gov/pubmed/21190553 http://dx.doi.org/10.1186/1471-2180-10-327 |
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author | Jani, Charul Eoh, Hyungjin Lee, Jae Jin Hamasha, Khozima Sahana, Moodakare Bheema Han, Jeong-Sun Nyayapathy, Seeta Lee, Jung-Yeon Suh, Joo-Won Lee, Sang Hee Rehse, Steve J Crick, Dean C Kang, Choong-Min |
author_facet | Jani, Charul Eoh, Hyungjin Lee, Jae Jin Hamasha, Khozima Sahana, Moodakare Bheema Han, Jeong-Sun Nyayapathy, Seeta Lee, Jung-Yeon Suh, Joo-Won Lee, Sang Hee Rehse, Steve J Crick, Dean C Kang, Choong-Min |
author_sort | Jani, Charul |
collection | PubMed |
description | BACKGROUND: Sensing and responding to environmental changes is a central aspect of cell division regulation. Mycobacterium tuberculosis contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases is Wag31, and we previously showed that partial depletion of Wag31 caused morphological changes indicative of cell wall defects, and that the phosphorylation state of Wag31 affected cell growth in mycobacteria. In the present study, we further characterized the role of the Wag31 phosphorylation in polar peptidoglycan biosynthesis. RESULTS: We demonstrate that the differential growth among cells expressing different wag31 alleles (wild-type, phosphoablative, or phosphomimetic) is caused by, at least in part, dissimilar nascent peptidoglycan biosynthesis. The phosphorylation state of Wag31 is found to be important for protein-protein interactions between the Wag31 molecules, and thus, for its polar localization. Consistent with these results, cells expressing a phosphomimetic wag31 allele have a higher enzymatic activity in the peptidoglycan biosynthetic pathway. CONCLUSIONS: The Wag31(Mtb )phosphorylation is a novel molecular mechanism by which Wag31(Mtb )regulates peptidoglycan synthesis and thus, optimal growth in mycobacteria. |
format | Text |
id | pubmed-3019181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30191812011-01-12 Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria Jani, Charul Eoh, Hyungjin Lee, Jae Jin Hamasha, Khozima Sahana, Moodakare Bheema Han, Jeong-Sun Nyayapathy, Seeta Lee, Jung-Yeon Suh, Joo-Won Lee, Sang Hee Rehse, Steve J Crick, Dean C Kang, Choong-Min BMC Microbiol Research Article BACKGROUND: Sensing and responding to environmental changes is a central aspect of cell division regulation. Mycobacterium tuberculosis contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases is Wag31, and we previously showed that partial depletion of Wag31 caused morphological changes indicative of cell wall defects, and that the phosphorylation state of Wag31 affected cell growth in mycobacteria. In the present study, we further characterized the role of the Wag31 phosphorylation in polar peptidoglycan biosynthesis. RESULTS: We demonstrate that the differential growth among cells expressing different wag31 alleles (wild-type, phosphoablative, or phosphomimetic) is caused by, at least in part, dissimilar nascent peptidoglycan biosynthesis. The phosphorylation state of Wag31 is found to be important for protein-protein interactions between the Wag31 molecules, and thus, for its polar localization. Consistent with these results, cells expressing a phosphomimetic wag31 allele have a higher enzymatic activity in the peptidoglycan biosynthetic pathway. CONCLUSIONS: The Wag31(Mtb )phosphorylation is a novel molecular mechanism by which Wag31(Mtb )regulates peptidoglycan synthesis and thus, optimal growth in mycobacteria. BioMed Central 2010-12-29 /pmc/articles/PMC3019181/ /pubmed/21190553 http://dx.doi.org/10.1186/1471-2180-10-327 Text en Copyright ©2010 Jani et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Jani, Charul Eoh, Hyungjin Lee, Jae Jin Hamasha, Khozima Sahana, Moodakare Bheema Han, Jeong-Sun Nyayapathy, Seeta Lee, Jung-Yeon Suh, Joo-Won Lee, Sang Hee Rehse, Steve J Crick, Dean C Kang, Choong-Min Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title | Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title_full | Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title_fullStr | Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title_full_unstemmed | Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title_short | Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria |
title_sort | regulation of polar peptidoglycan biosynthesis by wag31 phosphorylation in mycobacteria |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3019181/ https://www.ncbi.nlm.nih.gov/pubmed/21190553 http://dx.doi.org/10.1186/1471-2180-10-327 |
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