A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase

DC FieldValueLanguage
dc.contributor.authorvonderHaar, B
dc.contributor.authorWalter, S
dc.contributor.authorSchwapenheuer, S
dc.contributor.authorSchrempf, H
dc.date.accessioned2021-12-23T15:59:51Z-
dc.date.available2021-12-23T15:59:51Z-
dc.date.issued1997
dc.identifier.issn13500872
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4170-
dc.description.abstractResistance to fusidic acid in Streptomyces lividans is due to secretion of an extracellular enzyme (FusH) that converts the steroid antibiotic into an inactive derivative. NH2-terminal and several internal amino acid sequences were prepared from the purified enzyme. Using one of the deduced oligonucleotides to probe a subgenomic DNA library, the fusH gene was cloned and sequenced. Sequence analysis located an ORF which, owing to the presence of two putative start codons, indicates a predicted protein with 520 or 509 amino acids. A signal peptide was identified by aligning the deduced amino acids with the N-terminal sequence determined for the mature enzyme. The C-terminal part of the deduced FusH contains a region of three tandemly repeated stretches of 50 amino acids, which is preceded and followed by amino acids showing high homology with the repeats. FusH was found to share a CDS motif with some deduced esterases. S. lividans transformants carrying fusH on a multicopy vector synthesized high levels of FusH. Purified FusH cleaved equally well an acetyl, a thioacetyl or a formyl group from the 16 beta-position of fusidic acid and its derivatives. However, a propionyl group at the 16 beta-position was attacked with difficulty and a 16 alpha-acetyl group was not hydrolysed at all. These data indicate that FusH is a highly specific esterase. The fusH gene is widely distributed among streptomycetes that modify fusidic acid to its inactive lactone derivative.
dc.language.isoen
dc.publisherSOC GENERAL MICROBIOLOGY
dc.relation.ispartofMICROBIOLOGY-UK
dc.subjectDNA-SEQUENCE
dc.subjectESCHERICHIA-COLI
dc.subjectesterase (FusH)
dc.subjectEXPRESSION
dc.subjectFusH gene
dc.subjectfusidic-acid-inactivating enzyme
dc.subjectHYDROLASE
dc.subjectLIPASE
dc.subjectMicrobiology
dc.subjectMOLECULAR-CLONING
dc.subjectNUCLEOTIDE-SEQUENCE
dc.subjectPROTEIN
dc.subjectPURIFICATION
dc.subjectSIMILARITIES
dc.subjectStreptomyces lividans 66
dc.titleA novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase
dc.typejournal article
dc.identifier.doi10.1099/00221287-143-3-867
dc.identifier.isiISI:A1997WN28000021
dc.description.volume143
dc.description.issue3
dc.description.startpage867
dc.description.endpage874
dc.publisher.placeMARLBOROUGH HOUSE, BASINGSTOKE RD, SPENCERS WOODS, READING, BERKS, ENGLAND RG7 1AE
dcterms.isPartOf.abbreviationMicrobiology-(UK)
dcterms.oaStatusBronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidScHi752-
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