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Conference Paper: Versatile enzymatic system for the production of guanosine polyphosphates

TitleVersatile enzymatic system for the production of guanosine polyphosphates
Authors
KeywordsProtein
Staphylococcus aureus
Stringent response
Guanosine polyphosphate
Biosynthesis
Issue Date2010
PublisherSociety for General Microbiology.
Citation
The Apring 2010 Meeting of the Society for General Microbiology (SGM), Edinburgh, U.K., 29 March-1 April 2010. In Abstract Book of the SGM Spring 2010 Meeting, 2010, p. 99 How to Cite?
AbstractDuring periods of environmental stress, bacteria synthesize guanosine tetraphosphate (ppGpp, magic spot I) and guanosine pentaphosphate (pppGpp, magic spot II) in a process known as the stringent response. These intracellular allarmone molecules ‘reprogramme’ the transcriptional and translational machinery to help the cell conserve scarce resources. Existing methods for the production of guanosine polyphosphates are either technically difficult or inefficient, hindering investigations into their biological roles. We have developed a simple and efficient one-step enzymatic method for the production of guanosine polyphosphates using a recombinant protein cloned from Staphylococcus aureus. The purified enzyme efficiently catalyses the formation of pppGpp (and AMP) from GTP + ATP; and ppGpp (and AMP) from GDP + ATP. Notably, it also catalyses the synthesis of pGpp (guanosine 5’-monophosphate 3’-diphosphate, and AMP) from GMP + ATP; albeit with reduced efficiency. The reverse reactions are not catalysed, leading to high conversion rates. Guanosine polyphosphate products can be obtained in a homogeneous form using a combination of anion exchange chromatography followed by desalting. Our approach can be used to produce guanosine polyphosphates on a multi-milligram scale. Furthermore, our results also suggest that a third ‘magic spot’ allarmone may be formed within certain bacterial species.
DescriptionPosters - ED02 Signalling and systems biology: abstract no. ED02/20
Persistent Identifierhttp://hdl.handle.net/10722/129618

 

DC FieldValueLanguage
dc.contributor.authorChoi, MMYen_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorWatt, RMen_US
dc.date.accessioned2010-12-23T08:40:12Z-
dc.date.available2010-12-23T08:40:12Z-
dc.date.issued2010en_US
dc.identifier.citationThe Apring 2010 Meeting of the Society for General Microbiology (SGM), Edinburgh, U.K., 29 March-1 April 2010. In Abstract Book of the SGM Spring 2010 Meeting, 2010, p. 99en_US
dc.identifier.urihttp://hdl.handle.net/10722/129618-
dc.descriptionPosters - ED02 Signalling and systems biology: abstract no. ED02/20-
dc.description.abstractDuring periods of environmental stress, bacteria synthesize guanosine tetraphosphate (ppGpp, magic spot I) and guanosine pentaphosphate (pppGpp, magic spot II) in a process known as the stringent response. These intracellular allarmone molecules ‘reprogramme’ the transcriptional and translational machinery to help the cell conserve scarce resources. Existing methods for the production of guanosine polyphosphates are either technically difficult or inefficient, hindering investigations into their biological roles. We have developed a simple and efficient one-step enzymatic method for the production of guanosine polyphosphates using a recombinant protein cloned from Staphylococcus aureus. The purified enzyme efficiently catalyses the formation of pppGpp (and AMP) from GTP + ATP; and ppGpp (and AMP) from GDP + ATP. Notably, it also catalyses the synthesis of pGpp (guanosine 5’-monophosphate 3’-diphosphate, and AMP) from GMP + ATP; albeit with reduced efficiency. The reverse reactions are not catalysed, leading to high conversion rates. Guanosine polyphosphate products can be obtained in a homogeneous form using a combination of anion exchange chromatography followed by desalting. Our approach can be used to produce guanosine polyphosphates on a multi-milligram scale. Furthermore, our results also suggest that a third ‘magic spot’ allarmone may be formed within certain bacterial species.-
dc.languageengen_US
dc.publisherSociety for General Microbiology.-
dc.relation.ispartofAbstract Book of the SGM Spring 2010 Meetingen_US
dc.rightsAbstract Book of the SGM Spring 2010 Meeting. Copyright © Society for General Microbiology.-
dc.rightsThis is an author manuscript that has been accepted for publication in [Journal Title], copyright Society for General Microbiology, but has not been copy-edited, formatted or proofed. Cite this article as appearing in [Journal Title]. This version of the manuscript may not be duplicated or reproduced, other than for personal use or within the rule of 'Fair Use of Copyrighted Materials' (section 17, Title 17, US Code), without permission from the copyright owner, Society for General Microbiology. The Society for General Microbiology disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it by any other parties. The final copy-edited, published article, which is the version of record, can be found at [Journal URL], and is freely available without a subscription.-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectProtein-
dc.subjectStaphylococcus aureus-
dc.subjectStringent response-
dc.subjectGuanosine polyphosphate-
dc.subjectBiosynthesis-
dc.titleVersatile enzymatic system for the production of guanosine polyphosphatesen_US
dc.typeConference_Paperen_US
dc.identifier.emailChoi, MMY: meiychoi@hku.hken_US
dc.identifier.emailWang, Y: wangy727@gmail.comen_US
dc.identifier.emailWatt, RM: rmwatt@hku.hken_US
dc.identifier.authorityWatt, RM=rp00043en_US
dc.description.naturepostprint-
dc.identifier.hkuros177279en_US
dc.identifier.spage99-
dc.identifier.epage99-
dc.publisher.placeUnited Kingdom-
dc.description.otherThe Apring 2010 Meeting of the Society for General Microbiology (SGM), Edinburgh, U.K., 29 March-1 April 2010. In Abstract Book of the SGM Spring 2010 Meeting, 2010, p. 99-

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