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Article: Identification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4

TitleIdentification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4
Authors
Issue Date2000
PublisherAmerican Society for Microbiology.
Citation
Applied And Environmental Microbiology, 2000, v. 66 n. 8, p. 3180-3186 How to Cite?
AbstractHaloacid dehalogenases are enzymes that catalyze the hydrolytic removal of halogens from haloalkanoic acids. Dehalogenase IVa (DehIVa) from Burkholderia cepacia MBA4 and dehalogenase CI (DehCI) from Pseudomonas sp. strain CBS3 exhibit 68% identity. Despite their similarity DehIVa is a dimeric enzyme while DehCI is a monomer. In this work, we describe the identification of the domain that confers the dimerization function of DehIVa. Recombinant DNA molecules were constructed by fusion of the respective dehalogenase genes hdlIVa and dehCI. When amino acids 73 to 89 of DehCI were replaced by amino acids 74 to 90 of DehIVa, the recombinant molecule migrated like that of DehIVa in a nondenaturing activity-stained gel. Similarly, when residues 73 to 89 of DehIVa were replaced by the corresponding residues of DehCI the chimera migrated as a monomer. These 17 amino acid changes were able to determine the aggregation states of the molecules. The retention of the catalytic function in these chimeras indicated that the overall folding of these proteins was not affected. Site-directed mutagenesis on hdlIVa however indicated that amino acids Phe58, Thr65, Leu78, and Phe92 of DehIVa are also important for the aggregation state of the protein. This indicates that the 17 residues are not sufficient for the dimerization of the protein.
Persistent Identifierhttp://hdl.handle.net/10722/49000
ISSN
2015 Impact Factor: 3.823
2015 SCImago Journal Rankings: 1.891
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorPang, BCMen_HK
dc.date.accessioned2008-06-12T06:31:49Z-
dc.date.available2008-06-12T06:31:49Z-
dc.date.issued2000en_HK
dc.identifier.citationApplied And Environmental Microbiology, 2000, v. 66 n. 8, p. 3180-3186en_HK
dc.identifier.issn0099-2240en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49000-
dc.description.abstractHaloacid dehalogenases are enzymes that catalyze the hydrolytic removal of halogens from haloalkanoic acids. Dehalogenase IVa (DehIVa) from Burkholderia cepacia MBA4 and dehalogenase CI (DehCI) from Pseudomonas sp. strain CBS3 exhibit 68% identity. Despite their similarity DehIVa is a dimeric enzyme while DehCI is a monomer. In this work, we describe the identification of the domain that confers the dimerization function of DehIVa. Recombinant DNA molecules were constructed by fusion of the respective dehalogenase genes hdlIVa and dehCI. When amino acids 73 to 89 of DehCI were replaced by amino acids 74 to 90 of DehIVa, the recombinant molecule migrated like that of DehIVa in a nondenaturing activity-stained gel. Similarly, when residues 73 to 89 of DehIVa were replaced by the corresponding residues of DehCI the chimera migrated as a monomer. These 17 amino acid changes were able to determine the aggregation states of the molecules. The retention of the catalytic function in these chimeras indicated that the overall folding of these proteins was not affected. Site-directed mutagenesis on hdlIVa however indicated that amino acids Phe58, Thr65, Leu78, and Phe92 of DehIVa are also important for the aggregation state of the protein. This indicates that the 17 residues are not sufficient for the dimerization of the protein.en_HK
dc.format.extent384 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofApplied and Environmental Microbiologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsApplied and Environmental Microbiology. Copyright © American Society for Microbiology.en_HK
dc.rightsCopyright © American Society for Microbiology, Applied and Environmental Microbiology, 2000, v. 66 n. 8, p. 3180-3186en_HK
dc.subject.meshBurkholderia cepacia - chemistry - enzymology - geneticsen_HK
dc.subject.meshHydrolases - chemistry - genetics - metabolismen_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshDimerizationen_HK
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_HK
dc.titleIdentification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0099-2240&volume=66&issue=8&spage=3180&epage=3186&date=2000&atitle=Identification+of+the+dimerization+domain+of+dehalogenase+IVa+of+Burkholderia+cepacia+MBA4en_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1128/AEM.66.8.3180-3186.2000en_HK
dc.identifier.pmid10919767-
dc.identifier.pmcidPMC92131en_HK
dc.identifier.scopuseid_2-s2.0-0033863733en_HK
dc.identifier.hkuros53182-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033863733&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume66en_HK
dc.identifier.issue8en_HK
dc.identifier.spage3180en_HK
dc.identifier.epage3186en_HK
dc.identifier.isiWOS:000088546300008-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.scopusauthoridPang, BCM=36893364200en_HK

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