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

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

2015 John Wiley & Sons Ltd ;2015 John Wiley & Sons Ltd. ;2016 John Wiley & Sons Ltd ;ISSN: 0950-382X ;EISSN: 1365-2958 ;DOI: 10.1111/mmi.13281 ;PMID: 26585449

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Title:
Cyclic‐di‐AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in Lactococcus 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.
Subjects: Adenosine Monophosphate - metabolism ; Adenylyl Cyclases - metabolism ; Bacterial Proteins - metabolism ; Bacteriology ; Biosynthesis ; Cell Wall - metabolism ; Cyclic AMP - metabolism ; Dinucleoside Phosphates - biosynthesis ; Enzymes ; Lactococcus lactis - enzymology ; Lactococcus lactis - metabolism ; Mutation ; Peptides ; Peptidoglycan - biosynthesis ; Peptidoglycan - metabolism ; Phosphoglucomutase - metabolism ; Phosphoric Diester Hydrolases - metabolism ; Phosphorus-Oxygen Lyases - metabolism ; Second Messenger Systems
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 Firmicutes 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 Lactococcus. We characterized suppressor mutations that restored osmoresistance to spontaneous c‐di‐AMP phosphodiesterase gdpP mutants, which contain high c‐di‐AMP levels. Loss‐of‐function and gain‐of‐function mutations were identified in the cdaA and gdpP genes, respectively, which led to lower c‐di‐AMP levels. A mutation was also identified in the phosphoglucosamine mutase gene glmM, which is commonly located within the cdaA operon in bacteria. The glmM 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 GlmMI154F more than GlmM and GlmMI154F 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. c‐di‐AMP is an essential signalling molecule which affects peptidoglycan homeostasis and resistance against various stressors, however little is known regarding how the c‐di‐AMP level is regulated in the cell. Here we identify the peptidoglycan biosynthesis enzyme GlmM as a modulator of c‐di‐AMP synthesis through its regulation of diadenylate cyclase enzyme CdaA activity in Lactococcus lactis.
Publisher: England: Blackwell Publishing Ltd
Language: English
Identifier: ISSN: 0950-382X
EISSN: 1365-2958
DOI: 10.1111/mmi.13281
PMID: 26585449
Source: Geneva Foundation Free Medical Journals at publisher websites
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Cyclic‐di‐AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in Lactococcus lactis

2015 John Wiley & Sons Ltd ;2015 John Wiley & Sons Ltd. ;2016 John Wiley & Sons Ltd ;ISSN: 0950-382X ;EISSN: 1365-2958 ;DOI: 10.1111/mmi.13281 ;PMID: 26585449

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