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Conference Paper: Comparative functional analysis of bacterial small alarmone synthase proteins

TitleComparative functional analysis of bacterial small alarmone synthase proteins
Authors
Issue Date2014
PublisherSage Publications, Inc. The Journal's web site is located at http://jdr.sagepub.com/
Citation
The 28th Annual Scientific Meeting of the International Association for Dental Research Southeast Asian Division & 24th Annual Scientic Meeting, South East Asia Association For Dental Education (IADR-SEA/SEAADE 2014), Kuching, Malaysia, 13-14 August 2014. In Journal of Dental Research, 2014, v. 93 Spec. Iss. C, abstract no. 188 How to Cite?
AbstractObjective: During periods of nutritional or environmental stress, bacteria synthesize phosphorylated guanosine nucleotide derivatives known as alarmones. There are two major alarmones: guanosine tetraphosphate (ppGpp) and guanosine pentaphosphate (pppGpp). The (p)ppGpp molecules modulate a variety of intracellular processes in a coordinated manner known as the stringent response, to help the cell conserve and recycle essential resources. To characterize and compare the biochemical activities of a diverse set of proteins belonging to the ‘small alarmone synthase’ (SAS) family, to establish their putative roles in the production of (p)ppGpp alamone molecules. Method: Several SAS protein homologues from a variety of oral and systemic bacterial pathogens were cloned, expressed and purified. This included proteins encoded by relP and relQ genes from Fusobacterium nucleatum subsp. nucleatum, Staphylococcus aureus, Entereococcus faecalis and Streptococcus mutans. Their biochemical activities were characterized in vitro; focusing on their respective abilities to synthesize pppGpp, ppGpp and pGpp alarmones. Result: RelP and RelQ proteins from S. aureus, E. faecalis and S. mutans all possessed the ability to synthesize pppGpp, ppGpp and pGpp alamones; albeit with varying efficiencies. The single SAS encoded by F. nucleatum(RelQ, FN0926) primarily synthezied ppGpp, and to a lesser extent ppGpp, but lacked the ability to produce pGpp. All proteins lacked alarmone hydrolase activities. Conclusion: The biochemical activities of RelQ and RelP small alarmone synthase protein homologues vary considerably, suggesting that the major alamone molecules ppGpp and pppGpp are produced and utilized to differing extents within different bacterial species. Abstract Disclosures: This abstract is based on research that was funded entirely or partially by an outside source: Research Grants Council of Hong Kong, via a General Research Fund (GRF) grant #780112
Persistent Identifierhttp://hdl.handle.net/10722/225004
ISSN
2015 Impact Factor: 4.602
2015 SCImago Journal Rankings: 1.714

 

DC FieldValueLanguage
dc.contributor.authorYang, N-
dc.contributor.authorWatt, RM-
dc.contributor.authorLu, B-
dc.date.accessioned2016-04-18T03:35:16Z-
dc.date.available2016-04-18T03:35:16Z-
dc.date.issued2014-
dc.identifier.citationThe 28th Annual Scientific Meeting of the International Association for Dental Research Southeast Asian Division & 24th Annual Scientic Meeting, South East Asia Association For Dental Education (IADR-SEA/SEAADE 2014), Kuching, Malaysia, 13-14 August 2014. In Journal of Dental Research, 2014, v. 93 Spec. Iss. C, abstract no. 188-
dc.identifier.issn0022-0345-
dc.identifier.urihttp://hdl.handle.net/10722/225004-
dc.description.abstractObjective: During periods of nutritional or environmental stress, bacteria synthesize phosphorylated guanosine nucleotide derivatives known as alarmones. There are two major alarmones: guanosine tetraphosphate (ppGpp) and guanosine pentaphosphate (pppGpp). The (p)ppGpp molecules modulate a variety of intracellular processes in a coordinated manner known as the stringent response, to help the cell conserve and recycle essential resources. To characterize and compare the biochemical activities of a diverse set of proteins belonging to the ‘small alarmone synthase’ (SAS) family, to establish their putative roles in the production of (p)ppGpp alamone molecules. Method: Several SAS protein homologues from a variety of oral and systemic bacterial pathogens were cloned, expressed and purified. This included proteins encoded by relP and relQ genes from Fusobacterium nucleatum subsp. nucleatum, Staphylococcus aureus, Entereococcus faecalis and Streptococcus mutans. Their biochemical activities were characterized in vitro; focusing on their respective abilities to synthesize pppGpp, ppGpp and pGpp alarmones. Result: RelP and RelQ proteins from S. aureus, E. faecalis and S. mutans all possessed the ability to synthesize pppGpp, ppGpp and pGpp alamones; albeit with varying efficiencies. The single SAS encoded by F. nucleatum(RelQ, FN0926) primarily synthezied ppGpp, and to a lesser extent ppGpp, but lacked the ability to produce pGpp. All proteins lacked alarmone hydrolase activities. Conclusion: The biochemical activities of RelQ and RelP small alarmone synthase protein homologues vary considerably, suggesting that the major alamone molecules ppGpp and pppGpp are produced and utilized to differing extents within different bacterial species. Abstract Disclosures: This abstract is based on research that was funded entirely or partially by an outside source: Research Grants Council of Hong Kong, via a General Research Fund (GRF) grant #780112-
dc.languageeng-
dc.publisherSage Publications, Inc. The Journal's web site is located at http://jdr.sagepub.com/-
dc.relation.ispartofJournal of Dental Research-
dc.rightsJournal of Dental Research. Copyright © Sage Publications, Inc.-
dc.titleComparative functional analysis of bacterial small alarmone synthase proteins-
dc.typeConference_Paper-
dc.identifier.emailWatt, RM: rmwatt@hku.hk-
dc.identifier.authorityWatt, RM=rp00043-
dc.identifier.hkuros257452-
dc.identifier.volume93-
dc.identifier.issueSpec. Iss. C-
dc.publisher.placeUnited States-

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