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Conference Paper: Unraveling the members of a DNA-binding complex of a bacterial haloacid operon

TitleUnraveling the members of a DNA-binding complex of a bacterial haloacid operon
Authors
KeywordsBiology
Biochemistry
Issue Date2015
PublisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/
Citation
The 40th FEBS Congress, Berlin, Germany, 4-9 July 2015. In The FEBS Journal, 2015, v. 282 suppl. s1, p. 71, abstract P03-007 How to Cite?
AbstractHaloacetates are structurally simple organic acids that can be found in our environment. They are generated incidentally during disinfection of water and are mutagenic. A soil bacterium, Burkholderia caribensis strain MBA4, produces an inducible dehalogenase that transforms these compounds to utilizable substrates. Previous studies using electrophoretic mobility shift assay has identified at least two retardation complexes that bind to the upstream non-coding region of the dehalogenase gene. These complexes were detected in extracts prepared from glycolate-grown cells and not in haloacid-grown cultures. In this presentation, oligonucleotide-conjugated metal beads were used to capture these DNA-binding proteins. Candidates were subjected to tandem mass spectrometry assays and the gene encoding for a candidate was disrupted. When extracts prepared from this mutant was used, the formation of one of the retardation complexes was disabled. This candidate protein was heterologously expressed, purified and used for bandshift assay. Two retardation complexes, different from those identified in wildtype, were detected. When this purified recombinant protein was added to the extract of the mutant and used in bandshift assay, the missing complex was re-established. This candidate, tentatively named as Peg8620 has been identified as a member of TetR family of regulators. This suggested that the retardation complex being considered is formed by the interaction of Peg8620 and another protein.
DescriptionConference Theme: The Biochemical Basis of Life
Poster Sessions - Gen Ex S2, Turning Signals into Messages - the Complexity of Gene Regulation: no. P03-007
This free journal suppl. entitled: Special Issue: 40th FEBS Congress, The Biochemical Basis of Life ... 2015
Persistent Identifierhttp://hdl.handle.net/10722/212391
ISSN
2015 Impact Factor: 4.237
2015 SCImago Journal Rankings: 2.141

 

DC FieldValueLanguage
dc.contributor.authorDENG, L-
dc.contributor.authorTsang, JSH-
dc.date.accessioned2015-07-21T02:34:18Z-
dc.date.available2015-07-21T02:34:18Z-
dc.date.issued2015-
dc.identifier.citationThe 40th FEBS Congress, Berlin, Germany, 4-9 July 2015. In The FEBS Journal, 2015, v. 282 suppl. s1, p. 71, abstract P03-007-
dc.identifier.issn1742-464X-
dc.identifier.urihttp://hdl.handle.net/10722/212391-
dc.descriptionConference Theme: The Biochemical Basis of Life-
dc.descriptionPoster Sessions - Gen Ex S2, Turning Signals into Messages - the Complexity of Gene Regulation: no. P03-007-
dc.descriptionThis free journal suppl. entitled: Special Issue: 40th FEBS Congress, The Biochemical Basis of Life ... 2015-
dc.description.abstractHaloacetates are structurally simple organic acids that can be found in our environment. They are generated incidentally during disinfection of water and are mutagenic. A soil bacterium, Burkholderia caribensis strain MBA4, produces an inducible dehalogenase that transforms these compounds to utilizable substrates. Previous studies using electrophoretic mobility shift assay has identified at least two retardation complexes that bind to the upstream non-coding region of the dehalogenase gene. These complexes were detected in extracts prepared from glycolate-grown cells and not in haloacid-grown cultures. In this presentation, oligonucleotide-conjugated metal beads were used to capture these DNA-binding proteins. Candidates were subjected to tandem mass spectrometry assays and the gene encoding for a candidate was disrupted. When extracts prepared from this mutant was used, the formation of one of the retardation complexes was disabled. This candidate protein was heterologously expressed, purified and used for bandshift assay. Two retardation complexes, different from those identified in wildtype, were detected. When this purified recombinant protein was added to the extract of the mutant and used in bandshift assay, the missing complex was re-established. This candidate, tentatively named as Peg8620 has been identified as a member of TetR family of regulators. This suggested that the retardation complex being considered is formed by the interaction of Peg8620 and another protein.-
dc.languageeng-
dc.publisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/-
dc.relation.ispartofThe FEBS Journal-
dc.rightsPreprint This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article]. Authors are not required to remove preprints posted prior to acceptance of the submitted version. Postprint This is the accepted version of the following article: [full citation], which has been published in final form at [Link to final article].-
dc.subjectBiology-
dc.subjectBiochemistry-
dc.titleUnraveling the members of a DNA-binding complex of a bacterial haloacid operon-
dc.typeConference_Paper-
dc.identifier.emailTsang, JSH: jshtsang@hku.hk-
dc.identifier.authorityTsang, JSH=rp00792-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1111/febs.13339-
dc.identifier.hkuros245762-
dc.identifier.volume282-
dc.identifier.issuesuppl. s1-
dc.identifier.spage71, abstract P03-007-
dc.identifier.epage71, abstract P03-007-
dc.publisher.placeUnited Kingdom-

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