Amino acid residues involved in reversible thiol formation and zinc ion binding in the Streptomyces reticuli redox regulator FurS

DC FieldValueLanguage
dc.contributor.authorLucana, DOD
dc.contributor.authorTroller, M
dc.contributor.authorSchrempf, H
dc.date.accessioned2021-12-23T16:03:19Z-
dc.date.available2021-12-23T16:03:19Z-
dc.date.issued2003
dc.identifier.issn16174615
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5917-
dc.description.abstractStreptomyces reticuli produces a mycelium-associated enzyme, CpeB, whose N-terminal and C-terminal portions mediate heme-dependent catalase-peroxidase and heme-independent manganese-peroxidase activities, respectively. The regulator FurS governs transcription of the furS-cpeB operon. The thiol form of FurS contains one zinc ion per monomer and binds in this state to its cognate operator. Oxidation of SH groups within FurS induces the release of the zinc ion. Substitution of the codons for the amino acids cysteine 96, histidine 92 and 93, and tyrosine 59 in furs disrupts the in vivo repressor activity of FurS and results in enhanced synthesis of CpeB in corresponding S. lividans transformants. Biochemical and footprinting studies with FurS and its mutant derivatives revealed that the cysteine residues 96 and 99 are involved in reversible S-S bond formation, while cysteine 96 and the histidine residues 92 and 93 are required for zinc coordination, and tyrosine 59 is necessary for the binding of FurS to DNA. On the basis of these data, functional predictions can be made for the mycobacterial regulator FurA, a close homologue of FurS.
dc.language.isoen
dc.publisherSPRINGER-VERLAG
dc.relation.ispartofMOLECULAR GENETICS AND GENOMICS
dc.subjectANTI-SIGMA FACTOR
dc.subjectBiochemistry & Molecular Biology
dc.subjectCATALASE-PEROXIDASE GENE
dc.subjectCELLULASE AVICELASE
dc.subjectCpeB
dc.subjectDNA-BINDING
dc.subjectESCHERICHIA-COLI
dc.subjectGenetics & Heredity
dc.subjectmetalloregulator
dc.subjectMUTATIONAL ANALYSIS
dc.subjectMYCOBACTERIUM-TUBERCULOSIS
dc.subjectOXYR TRANSCRIPTION FACTOR
dc.subjectredox regulator protein
dc.subjectSENSITIVE METHOD
dc.subjectStreptomycetes
dc.subjectthiol-reduced FurS
dc.subjectUPTAKE REGULATION PROTEIN
dc.titleAmino acid residues involved in reversible thiol formation and zinc ion binding in the Streptomyces reticuli redox regulator FurS
dc.typejournal article
dc.identifier.doi10.1007/s00438-002-0776-0
dc.identifier.isiISI:000181616000006
dc.description.volume268
dc.description.issue5
dc.description.startpage618
dc.description.endpage627
dc.publisher.place175 FIFTH AVE, NEW YORK, NY 10010 USA
dcterms.isPartOf.abbreviationMol. Genet. Genomics
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidScHi752-
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