The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS

DC FieldValueLanguage
dc.contributor.authorZou, PJ
dc.contributor.authorBorovok, I
dc.contributor.authorLucana, DOD
dc.contributor.authorMuller, D
dc.contributor.authorSchrempf, H
dc.date.accessioned2021-12-23T15:59:50Z-
dc.date.available2021-12-23T15:59:50Z-
dc.date.issued1999
dc.identifier.issn13500872
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4162-
dc.description.abstractDuring early stages of growth, Streptomyces reticuli synthesizes a hyphae-associated, haem-containing enzyme which exhibits catalase and peroxidase activities with broad substrate specificity (CpeB). The purified dimeric enzyme (160 kDa) consists of two identical subunits. Using anti-CpeB antibodies and an expression- as well as a mini-library, the corresponding cpeB gene was identified and sequenced. It encodes a protein of 740 aa with a molecular mass of 81.3 kDa. The deduced protein shares the highest level of amino acid identity with KatG from Caulobacter crescentus and Mycobacterium tuberculosis, and PerA from Bacillus stearothermophilus. Streptomyces lividans transformants carrying cpeB and the upstream-located furS gene with its regulatory region on the bifunctional vector pWHM3 produced low or enhanced levels of CpeB in the presence or absence of Fe ions, respectively. An in-frame deletion of the major part of furS induces increased CpeB synthesis. The data imply that FurS regulates the transcription of cpeB. The deduced FurS protein is rich in histidine residues, contains a putative N-terminally situated helix-turn-helix motif and has a molecular mass of 15.1 kDa. It shares only 29% amino acid identity with the Escherichia coli ferric uptake regulator (Fur) protein, but about 64% with FurA deduced from the genomic sequences of several mycobacteria. The predicted secondary structures of FurS and FurA are highly similar and considerably divergent from those of the E. coli Fur. In contrast to some Gram-negative bacteria, within several mycobacteria an intact furA gene or a furA pseudogene is upstream of a catalase-peroxidase (katG) gene predicted to encode a functional or a non-functional (Mycobacterium leprae) enzyme. Thus the data obtained for Streptomyces reticuli are expected to serve as an additional model to elucidate the regulation of mycobacterial catalase-peroxidase genes.
dc.language.isoen
dc.publisherSOC GENERAL MICROBIOLOGY
dc.relation.ispartofMICROBIOLOGY-SGM
dc.subjectACTIVATION
dc.subjectcatalase-peroxidase genes
dc.subjectCELLULASE AVICELASE
dc.subjectCLONING
dc.subjectCRYSTAL-STRUCTURE
dc.subjectESCHERICHIA-COLI
dc.subjectFur proteins
dc.subjectIRON
dc.subjectMicrobiology
dc.subjectmycobacteria
dc.subjectMYCOBACTERIUM-TUBERCULOSIS
dc.subjectPURIFICATION
dc.subjectREPRESSOR PROTEIN
dc.subjectSEQUENCE-ANALYSIS
dc.subjectstreptomycetes
dc.titleThe mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS
dc.typejournal article
dc.identifier.doi10.1099/13500872-145-3-549
dc.identifier.isiISI:000079099500006
dc.description.volume145
dc.description.issue3
dc.description.startpage549
dc.description.endpage559
dc.contributor.orcid0000-0003-1602-4499
dc.publisher.placeMARLBOROUGH HOUSE, BASINGSTOKE RD, SPENCERS WOODS, READING RG7 1AG, BERKS, ENGLAND
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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