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Article: Sec-dependent and Sec-independent translocation of haloacid dehalogenase Chd1 of Burkholderia cepacia MBA4 in Escherichia coli

TitleSec-dependent and Sec-independent translocation of haloacid dehalogenase Chd1 of Burkholderia cepacia MBA4 in Escherichia coli
Authors
KeywordsBurkholderia cepacia
Green fluorescent protein
L-2-Haloacid dehalogenase
Protein translocation
Issue Date2002
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1
Citation
Fems Microbiology Letters, 2002, v. 211 n. 2, p. 259-264 How to Cite?
Abstract2-Haloacid dehalogenases are hydrolytic enzymes that cleave the halogen-carbon bond(s) in haloalkanoic acids. We have previously isolated a cryptic haloacid dehalogenase gene from Burkholderia cepacia MBA4 and expressed it in Escherichia coli. This recombinant protein is unusual in having a long leader sequence, a property of periplasmic enzymes. In this paper, we report the functional role of this leader sequence. Western blot analyses showed that Chd1 is translocated to the periplasm. The results on the expression of Chd1 in the presence of sodium azide suggested the cleavage of the leader to be Sec-dependent. Chimeras of Chd1 and green fluorescent protein demonstrated that the leader sequence is fully functional in translocating the fusion protein to the periplasm. The expression of the chimeras in Sec mutants supported the Sec-dependent translocation. Surprisingly, recombinant Chd1 and a chimera with no leader sequence were also found in the periplasm. © 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Microbiological Societies.
Persistent Identifierhttp://hdl.handle.net/10722/68645
ISSN
2015 Impact Factor: 1.858
2015 SCImago Journal Rankings: 1.126
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorSze, Jen_HK
dc.date.accessioned2010-09-06T06:06:25Z-
dc.date.available2010-09-06T06:06:25Z-
dc.date.issued2002en_HK
dc.identifier.citationFems Microbiology Letters, 2002, v. 211 n. 2, p. 259-264en_HK
dc.identifier.issn0378-1097en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68645-
dc.description.abstract2-Haloacid dehalogenases are hydrolytic enzymes that cleave the halogen-carbon bond(s) in haloalkanoic acids. We have previously isolated a cryptic haloacid dehalogenase gene from Burkholderia cepacia MBA4 and expressed it in Escherichia coli. This recombinant protein is unusual in having a long leader sequence, a property of periplasmic enzymes. In this paper, we report the functional role of this leader sequence. Western blot analyses showed that Chd1 is translocated to the periplasm. The results on the expression of Chd1 in the presence of sodium azide suggested the cleavage of the leader to be Sec-dependent. Chimeras of Chd1 and green fluorescent protein demonstrated that the leader sequence is fully functional in translocating the fusion protein to the periplasm. The expression of the chimeras in Sec mutants supported the Sec-dependent translocation. Surprisingly, recombinant Chd1 and a chimera with no leader sequence were also found in the periplasm. © 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Microbiological Societies.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1en_HK
dc.relation.ispartofFEMS Microbiology Lettersen_HK
dc.rightsF E M S Microbiology Letters. Copyright © Blackwell Publishing Ltd.en_HK
dc.subjectBurkholderia cepaciaen_HK
dc.subjectGreen fluorescent proteinen_HK
dc.subjectL-2-Haloacid dehalogenaseen_HK
dc.subjectProtein translocationen_HK
dc.titleSec-dependent and Sec-independent translocation of haloacid dehalogenase Chd1 of Burkholderia cepacia MBA4 in Escherichia colien_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0378-1097&volume=211&spage=259&epage=264&date=2002&atitle=Sec-dependent+and+Sec-independent+translocation+of+haloacid+dehalogenase+Chd1+of+Burkholderia+cepacia+MBA4+in+Escherichia+colien_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0378-1097(02)00702-4en_HK
dc.identifier.pmid12076822-
dc.identifier.scopuseid_2-s2.0-0037018904en_HK
dc.identifier.hkuros66550en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037018904&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume211en_HK
dc.identifier.issue2en_HK
dc.identifier.spage259en_HK
dc.identifier.epage264en_HK
dc.identifier.isiWOS:000176448600022-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.scopusauthoridSze, J=36834949600en_HK

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