Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis

Cyclic di-AMP (c-di-AMP) is a recently discovered bacterial secondary messenger molecule, which is associated with various physiological functions. In Bacillus, the intracellular level and turnover of c-di-AMP is mainly regulated by three diadenylate cyclases (DACs), including DisA, CdaA and CdaS, a...

Full description

Bibliographic Details
Main Authors: Cao eZheng, Yang eMa, Xun eWang, Yuqun eXie, Maria Kanwal Ali, Jin eHe
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-09-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00908/full
_version_ 1819238720379813888
author Cao eZheng
Yang eMa
Xun eWang
Yuqun eXie
Maria Kanwal Ali
Jin eHe
author_facet Cao eZheng
Yang eMa
Xun eWang
Yuqun eXie
Maria Kanwal Ali
Jin eHe
author_sort Cao eZheng
collection DOAJ
description Cyclic di-AMP (c-di-AMP) is a recently discovered bacterial secondary messenger molecule, which is associated with various physiological functions. In Bacillus, the intracellular level and turnover of c-di-AMP is mainly regulated by three diadenylate cyclases (DACs), including DisA, CdaA and CdaS, and one c-di-AMP-specific phosphodiesterase. In this study, we demonstrated that CdaS protein from B. thuringiensisis is a hexameric DAC protein that can convert ATP or ADP to c-di-AMP in vitro and the N-terminal YojJ domain was essential for the DAC activity. Based on the markerless gene knock-out method, we demonstrated that the transcription of cdaS was initiated by the sporulation-specific sigma factor σH and the deletion of cdaS significantly delayed sporulation and parasporal crystal formation. These findings contrast with similar experiments conducted using B. subtilis, wherein transcription of its cdaS was initiated by the sigma factor σG. Deletion of all the three DAC genes from a single strain was unsuccessful, suggesting that c-di-AMP is an indispensable molecule in B. thuringiensis. Phylogenetic analysis indicated increased diversity of CdaS in the B. cereus and B. subtilis Bacillus subgroups. In summary, this study identifies important aspects in the regulation of c-di-AMP in Bacillus.
first_indexed 2024-12-23T13:40:43Z
format Article
id doaj.art-4970162d138444e5bfa187a438b3df7c
institution Directory Open Access Journal
issn 1664-302X
language English
last_indexed 2024-12-23T13:40:43Z
publishDate 2015-09-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Microbiology
spelling doaj.art-4970162d138444e5bfa187a438b3df7c2022-12-21T17:44:52ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-09-01610.3389/fmicb.2015.00908154118Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensisCao eZheng0Yang eMa1Xun eWang2Yuqun eXie3Maria Kanwal Ali4Jin eHe5Huazhong agricultural universityHuazhong agricultural universityHuazhong agricultural universityHubei University of TechnologyHuazhong agricultural universityHuazhong agricultural universityCyclic di-AMP (c-di-AMP) is a recently discovered bacterial secondary messenger molecule, which is associated with various physiological functions. In Bacillus, the intracellular level and turnover of c-di-AMP is mainly regulated by three diadenylate cyclases (DACs), including DisA, CdaA and CdaS, and one c-di-AMP-specific phosphodiesterase. In this study, we demonstrated that CdaS protein from B. thuringiensisis is a hexameric DAC protein that can convert ATP or ADP to c-di-AMP in vitro and the N-terminal YojJ domain was essential for the DAC activity. Based on the markerless gene knock-out method, we demonstrated that the transcription of cdaS was initiated by the sporulation-specific sigma factor σH and the deletion of cdaS significantly delayed sporulation and parasporal crystal formation. These findings contrast with similar experiments conducted using B. subtilis, wherein transcription of its cdaS was initiated by the sigma factor σG. Deletion of all the three DAC genes from a single strain was unsuccessful, suggesting that c-di-AMP is an indispensable molecule in B. thuringiensis. Phylogenetic analysis indicated increased diversity of CdaS in the B. cereus and B. subtilis Bacillus subgroups. In summary, this study identifies important aspects in the regulation of c-di-AMP in Bacillus.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00908/fullBacillus thuringiensissporulationCDAsParasporal crystalCyclic di-AMP
spellingShingle Cao eZheng
Yang eMa
Xun eWang
Yuqun eXie
Maria Kanwal Ali
Jin eHe
Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
Frontiers in Microbiology
Bacillus thuringiensis
sporulation
CDAs
Parasporal crystal
Cyclic di-AMP
title Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
title_full Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
title_fullStr Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
title_full_unstemmed Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
title_short Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
title_sort functional analysis of the sporulation specific diadenylate cyclase cdas in bacillus thuringiensis
topic Bacillus thuringiensis
sporulation
CDAs
Parasporal crystal
Cyclic di-AMP
url http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00908/full
work_keys_str_mv AT caoezheng functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis
AT yangema functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis
AT xunewang functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis
AT yuqunexie functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis
AT mariakanwalali functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis
AT jinehe functionalanalysisofthesporulationspecificdiadenylatecyclasecdasinbacillusthuringiensis