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Article: Characterization, heterologous expression and functional analysis of mevalonate diphosphate decarboxylase gene (MVD) of Candida albicans

TitleCharacterization, heterologous expression and functional analysis of mevalonate diphosphate decarboxylase gene (MVD) of Candida albicans
Authors
Issue Date2002
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00438/index.htm
Citation
Molecular Genetics And Genomics, 2002, v. 267 n. 3, p. 281-290 How to Cite?
AbstractMevalonate diphosphate decarboxylase (MVD) catalyzes the conversion of mevalonate diphosphate to isopentenyl diphosphate, a key building block for a large family of functionally important biomolecules. We have cloned the gene encoding MVD from Candida albicans, and report the first characterization of such a gene from an opportunistic fungal pathogen. Sequence analysis revealed that the MVD comprises 362 amino acid residues with a predicted molecular weight of 39.5 kDa, sharing minimal identity with the human analogue. Analysis of the genomic sequence indicated that the coding frame is interrupted by a small intron of 51 bp. Southern analysis of genomic DNA demonstrated that MVD is a single-copy gene. Furthermore, Southern analysis of electrophoretic karyotypes of C. albicans obtained by pulsed-field gel electrophoresis showed that MVD is located on chromosome 1. Northern analysis revealed that the level of MVD expression is affected by (1) the carbon source in the growth medium, (2) the growth phase, and (3) the growth form of the fungus (yeast-like or hyphal). To demonstrate the biological function of C. albicans MVD, complementation experiments were carried out with an S. cerevisiae strain (erg19ts) that is temperature-sensitive for MVD activity. A single copy of the C. albicans MVD gene, under the control of the NOP1 promoter, was able fully to complement the erg19ts phenotype, and expression of the epitope-tagged C. albicans MVD was detectable by Western analysis. Furthermore, the low degree of sequence identity between C. albicans MVD and its human analogue raises the possibility that fungal-specific inhibitors can be developed for the enzyme. Thus, C. albicans MVD appears to be an interesting candidate that could be targeted for the development of anti-fungal agents.
Persistent Identifierhttp://hdl.handle.net/10722/66869
ISSN
2015 Impact Factor: 2.622
2015 SCImago Journal Rankings: 1.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDassanayake, Ren_HK
dc.contributor.authorCao, Len_HK
dc.contributor.authorSamaranayake, Len_HK
dc.contributor.authorBerges, Ten_HK
dc.date.accessioned2010-09-06T05:50:02Z-
dc.date.available2010-09-06T05:50:02Z-
dc.date.issued2002en_HK
dc.identifier.citationMolecular Genetics And Genomics, 2002, v. 267 n. 3, p. 281-290en_HK
dc.identifier.issn1617-4615en_HK
dc.identifier.urihttp://hdl.handle.net/10722/66869-
dc.description.abstractMevalonate diphosphate decarboxylase (MVD) catalyzes the conversion of mevalonate diphosphate to isopentenyl diphosphate, a key building block for a large family of functionally important biomolecules. We have cloned the gene encoding MVD from Candida albicans, and report the first characterization of such a gene from an opportunistic fungal pathogen. Sequence analysis revealed that the MVD comprises 362 amino acid residues with a predicted molecular weight of 39.5 kDa, sharing minimal identity with the human analogue. Analysis of the genomic sequence indicated that the coding frame is interrupted by a small intron of 51 bp. Southern analysis of genomic DNA demonstrated that MVD is a single-copy gene. Furthermore, Southern analysis of electrophoretic karyotypes of C. albicans obtained by pulsed-field gel electrophoresis showed that MVD is located on chromosome 1. Northern analysis revealed that the level of MVD expression is affected by (1) the carbon source in the growth medium, (2) the growth phase, and (3) the growth form of the fungus (yeast-like or hyphal). To demonstrate the biological function of C. albicans MVD, complementation experiments were carried out with an S. cerevisiae strain (erg19ts) that is temperature-sensitive for MVD activity. A single copy of the C. albicans MVD gene, under the control of the NOP1 promoter, was able fully to complement the erg19ts phenotype, and expression of the epitope-tagged C. albicans MVD was detectable by Western analysis. Furthermore, the low degree of sequence identity between C. albicans MVD and its human analogue raises the possibility that fungal-specific inhibitors can be developed for the enzyme. Thus, C. albicans MVD appears to be an interesting candidate that could be targeted for the development of anti-fungal agents.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00438/index.htmen_HK
dc.relation.ispartofMolecular Genetics and Genomicsen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshCandida albicans - enzymology - geneticsen_HK
dc.subject.meshCarboxy-Lyases - genetics - metabolismen_HK
dc.subject.meshCloning, Molecularen_HK
dc.subject.meshGenetic Complementation Testen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshPhylogenyen_HK
dc.subject.meshSaccharomyces cerevisiae - metabolismen_HK
dc.subject.meshSequence Analysis, DNAen_HK
dc.titleCharacterization, heterologous expression and functional analysis of mevalonate diphosphate decarboxylase gene (MVD) of Candida albicansen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0026-8925&volume=&spage=&epage=&date=2002&atitle=Characterization,+heterologous+expression+and+functional+analysis+of+mevalonate+diphosphate+decarboxylase+gene+(MVD)+of+Candida+albicansen_HK
dc.identifier.emailSamaranayake, L:lakshman@hku.hken_HK
dc.identifier.authoritySamaranayake, L=rp00023en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s00438-002-0648-7en_HK
dc.identifier.pmid12073030en_HK
dc.identifier.scopuseid_2-s2.0-0036273913en_HK
dc.identifier.hkuros65793en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036273913&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume267en_HK
dc.identifier.issue3en_HK
dc.identifier.spage281en_HK
dc.identifier.epage290en_HK
dc.identifier.isiWOS:000176530600002-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridDassanayake, R=6603321318en_HK
dc.identifier.scopusauthoridCao, L=7401637818en_HK
dc.identifier.scopusauthoridSamaranayake, L=7102761002en_HK
dc.identifier.scopusauthoridBerges, T=6603743338en_HK

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