Regulation of gene expression by oxygen in Saccharomyces cerevisiae.

Zitomer, R S; Lowry, Charles V.

doi:10.1128/mmbr.56.1.1-11.1992

Cited by 257 publications

(188 citation statements)

References 73 publications

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“…Other regulatory elements in the promoter region of the quinol oxidase are a FnrP consensus sequence [34] as well as a binding motif for a heme-activated protein [35] like the one observed upstream of the cytochrome csso gene [36], both possibly involved in oxygen regulation. Analysis (not shown) of the position of the transcriptional start suggests that the FnrP site is superimposed on the qox operon promoter which would indicate some inhibitory effect of FnrP binding, while the heme-activated protein site should be functional under aerobic conditions with respect to its location relative to the proposed promoter region (Fig.…”

Section: Discussionmentioning

confidence: 99%

Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive

Zickermann¹,

Tautu²,

Link³

et al. 1997

European Journal of Biochemistry

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Expression of the quinol oxidase from Paracoccus denitrijicans has been examined using a polyclonal antibody directed against subunit I1 and a promoter probe vector carrying the promoter region of the qox operon. Under aerobic conditions nitrate and nitrite act as specific inducers of the expression. To obtain an enzymatically competent quinol oxidase complex, an intact ctaB gene is required, which constitutes part of the eta operon coding for the aa, cytochrome c oxidase of P: denitrificans. Deletion of ctaB leads to a change in heme composition of the quinol oxidase with heme b replacing the high-spin heme a of the binuclear center, causing loss of electron transport activity.Keywords : cytochrome-c oxidase ; high-spin heme ; CtaB ; nitratehitrite regulation ; NarL. [2] proposed a different heme composition. When they analyzed the heme composition of membranes isolated from a strain deleted in both copies of the aa, subunit I genes they concluded that both heme sites of the remaining quinol oxidase are occupied by b-type hemes. This discrepancy in the reported heme composition was explained by a different genetic background of the respective Paracoccus strains [2].In this report we present expression studies of the quinol oxidase in different strains as well as the characterization of the purified enzymes from these strains. The heme composition of the quinol oxidase is changed by deletion of the cta operon as can be seen from visible absorption and magnetic circular dichroism (MCD) spectroscopic analysis. MATERIALS AND METHODSPlasmids, bacteria and growth condition. Paracoccus denitri,fcans strains Pd1222 [ 181, (3440 (deletion of the f l c operon coding for the cytochrome be, complex, dfbc::neo) [19], ST4 (lacking the complete eta operon, dcta::neo) and ST4P (ST4 complemented with ctaC and ctaB in trans) [14] were grown aerobically on succinate medium, which was supplemented with KNO, or KNO, where indicated. P: denitrificans cells were harvested in the logarithmic growth phase, disrupted and membranes isolated as described previously [20]. Anaerobic cultures were grown in stoppered flasks with a paraffin oil overlay. E. coli cells were cultured in TY medium (0.8 % tryptone, 0.5 % yeast extract, 0.5% NaCI, pH 7.3), treated with lysozyme, and subsequently disrupted by sonication.The cytochrome ba, promoter region was amplified from an EcoRI fragment of the qox operon (position -339 to +257) cloned into pUC18 (reverse primer and primer MU2: 5'-TCTA-GATGTACATCATTGGACTACCCG-?) as was the genetically engineered E. COli P-galactosidase gene (universal primer and primer MG 1 : S-TTGGTACCAATGTACAAGGTTTTATCCGCorrespondence to 0.

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Section: Discussionmentioning

confidence: 99%

Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive

Zickermann¹,

Tautu²,

Link³

et al. 1997

European Journal of Biochemistry

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“…By comparison with upper activating sequences (UAS), homology was found between HAP1 binding sites and ORE sequences. HAP1 (heme activating protein) is known to be involved in gene activation and also in repression of mitochondrial yeast proteins [169]. Heme-controlled gene expression of cytochrome oxidase in yeast has long been known [170] to be an essential step in biogenesis control [169,171].…”

Section: Homology Of Ore Elements To Heme Activating Protein (Hap) Bimentioning

confidence: 99%

Genetics of Paracoccus denitrificans

Steinrücke

Ludwig

1993

FEMS Microbiology Letters

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Paracoccus has approx. 15 subunits [28]. The transcriptional organization of this NDH-l-cluster is presently unknown. NQ01 and NQ02 code for flavoproteins, NQ03 to NQ06 are genes for iron-sulfur proteins whereas NQ07 to NQ014 code for polypeptides of the hydrophobic protein fraction [28]. The gene order in this cluster is NQ07, NQ06, NQ05, NQ04, NO02, NQ01 NQ03, NQ08 NQ09, NQ010, NQ011, NQO12, NQ013, and NQ014.Upstream of NQ07 an open reading frame with homology to Escherichia coli uvrA is found. A reading frame with homology to E. coli biotin acetyl-CoA carboxylase ligase has been found downstream of the cluster [28].Sequences for two genes, NQ01 [29], encoding the NADH-binding subunit, and NQ02 [30], which codes for an iron-sulfur protein, have been published. Two URFs have been found; sequence similarities of URF2 to ctaG of the Paracoccus cta-operon suggest a possible role as an assembly protein, most probably in the attachment of iron [29,30,55]. Because of its simpler structure the Paracoccus complex is likely to play an important part in investigating inhibitory agents or the mode of complex formation during assembly. Mutant strains are presently not available.

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“…Similar octanucleotide sequences, with the consensus 5'-TNRTTGGT-3', have been found in a number of nuclear genes encoding mitochondrial proteins in mammals and yeast, where they have been proposed to be the responsive element for the transcription activation factor HAP2/3/4 [ 151. This observation raises the possibility of a regulation of the COX-V gene by heme and the carbon source [16]. Moreover, the presence of the octamer in slime mold, an organism distantly related to both yeast and mammals, seems to add further support to the idea that this element might represent a signature of nuclear genes for mitochondrial proteins involved in respiratory functions [17].…”

Section: Promoter Activity Of the 5'-flanking Regionmentioning

confidence: 99%

Structure of the promoter region of the gene encoding cytochrome c oxidase subunit V in Dictyostelium

Rizzuto

Sandonà

Brini

et al. 1993

European Journal of Biochemistry

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A cDNA for the nuclear‐encoded subunit V of Dictyostelium discoideum cytochrome‐c oxidase was used as a probe to screen a genomic library and isolate the complete gene. Primer‐extension analysis revealed two transcription start sites located 32 and 39 nucleotides upstream of the translation intiation codon. The chloramphenicol acetyltransferase assay in transient and stable Dictyostelium transformants indicated that the 400‐bp dT‐rich segment 5′ to the transcription start sites retained promoter activity. This region contains an octanucleotide sequence similar to the yeast HAP2/3/4 responsive element.

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Regulation of gene expression by oxygen in Saccharomyces cerevisiae.

Cited by 257 publications

References 73 publications

Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive

Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive

Genetics of Paracoccus denitrificans

Structure of the promoter region of the gene encoding cytochrome c oxidase subunit V in Dictyostelium

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Regulation of gene expression by oxygen in Saccharomyces cerevisiae.

Cited by 257 publications

References 73 publications

Expression Studies on the ba3 Quinol Oxidase from Paracoccus Denitrificans A bb3 Variant is Enzymatically Inactive

Expression Studies on the ba3 Quinol Oxidase from Paracoccus Denitrificans A bb3 Variant is Enzymatically Inactive

Genetics of Paracoccus denitrificans

Structure of the promoter region of the gene encoding cytochrome c oxidase subunit V in Dictyostelium

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Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive

Expression Studies on the ba₃ Quinol Oxidase from Paracoccus Denitrificans A bb₃ Variant is Enzymatically Inactive