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Cyclic‐di‐ AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in L actococcus lactis

Molecular microbiology, 2016-03, Vol.99 (6), p.1015-1027 [Peer Reviewed Journal]

ISSN: 0950-382X ;EISSN: 1365-2958 ;DOI: 10.1111/mmi.13281

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  • Title:
    Cyclic‐di‐ AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in L actococcus lactis
  • Author: Zhu, Yan ; Pham, Thi Huong ; Nhiep, Thi Hanh Nguyen ; Vu, Ngoc Minh Thu ; Marcellin, Esteban ; Chakrabortti, Alolika ; Wang, Yuanliang ; Waanders, Jennifer ; Lo, Raquel ; Huston, Wilhelmina M. ; Bansal, Nidhi ; Nielsen, Lars K. ; Liang, Zhao‐Xun ; Turner, Mark S.
  • Is Part Of: Molecular microbiology, 2016-03, Vol.99 (6), p.1015-1027
  • Description: Summary The second messenger cyclic‐di‐adenosine monophosphate ( c‐di‐AMP ) plays important roles in growth, virulence, cell wall homeostasis, potassium transport and affects resistance to antibiotics, heat and osmotic stress. Most F irmicutes contain only one c‐di‐ AMP synthesizing diadenylate cyclase ( CdaA ); however, little is known about signals and effectors controlling CdaA activity and c‐di‐ AMP levels. In this study, a genetic screen was employed to identify components which affect the c‐di‐ AMP level in L actococcus . We characterized suppressor mutations that restored osmoresistance to spontaneous c‐di‐ AMP phosphodiesterase gdp P mutants, which contain high c‐di‐ AMP levels. Loss‐of‐function and gain‐of‐function mutations were identified in the cda A and gdp P genes, respectively, which led to lower c‐di‐ AMP levels. A mutation was also identified in the phosphoglucosamine mutase gene glm M , which is commonly located within the cda A operon in bacteria. The glm M I154F mutation resulted in a lowering of the c‐di‐ AMP level and a reduction in the key peptidoglycan precursor UDP ‐ N ‐acetylglucosamine in L . lactis . C‐di‐ AMP synthesis by CdaA was shown to be inhibited by GlmM I154F more than GlmM and Glm M I154F was found to bind more strongly to CdaA than GlmM . These findings identify GlmM as a c‐di‐ AMP level modulating protein and provide a direct connection between c‐di‐ AMP synthesis and peptidoglycan biosynthesis.
  • Language: English
  • Identifier: ISSN: 0950-382X
    EISSN: 1365-2958
    DOI: 10.1111/mmi.13281
  • Source: GFMER Free Medical Journals
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