Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae

Guarente, Leonard; Lalonde, Beth A.; Gifford, Paula; Alani, Eric

doi:10.1016/0092-8674(84)90243-5

Cited by 486 publications

(349 citation statements)

References 18 publications

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“…A similar regulation has been found for several other mitochondrial proteins. In the case of the CYCl gene which encodes iso-1-cytochrome c [2, 31, regulation appears to be mediated by two discrete, tandem upstream activation sites, UASl and UAS2, located at about -337 and -291, respectively, from the ATG start codon [3]. Although these sites are similar in sequence, their regulatory function appears to be different [3].…”

Section: Conserved Sequence Elements Upstream Of the M N Superoxide Dmentioning

confidence: 99%

“…In the case of the CYCl gene which encodes iso-1-cytochrome c [2, 31, regulation appears to be mediated by two discrete, tandem upstream activation sites, UASl and UAS2, located at about -337 and -291, respectively, from the ATG start codon [3]. Although these sites are similar in sequence, their regulatory function appears to be different [3]. Interestingly, sequences similar to the CYCl-UAS are present upstream of the Mn superoxide dismutase gene (Table 1) and, although the functional importance of these has yet to be assessed, it may be significant that the Mn superoxide dismutase gene is expressed in parallel with the CYCl gene in a mutant that exhibits constitutivity of the latter gene under anaerobic conditions [55].…”

Section: Conserved Sequence Elements Upstream Of the M N Superoxide Dmentioning

confidence: 99%

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Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron‐sulphur protein

Marres¹,

Loon

Oudshoorn³

et al. 1985

European Journal of Biochemistry

126

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We have previously reported the isolation of the gene coding for a 25‐kDa polypeptide present in a purified yeast QH2:cytochrome c oxidoreductase preparation, which was thus identified as the gene for the Rieske ironsulphur protein [Van Loon et al. (1983) Gene 26, 261–272]. Subsequent DNA sequence analysis reported here reveals, however, that the encoded protein is in fact manganese superoxide dismutase, a mitochondrial matrix protein. Comparison with the known amino acid sequence of the mature protein indicates that it is synthesized with an N‐terminal extension of 27 amino acids. In common with the N‐terminal extensions of other imported mitochondrial proteins, the presequence has several basic residues but lacks negatively charged residues. The function of these positive charges and other possible topogenic sequences are discussed. Sequences 5′ of the gene contain two elements that may be homologous to the suggested regulatory sites, UAS 1 and UAS 2 in the yeast CYC1‐gene [Guarente et al. (1984) Cell 36, 503–511]. The predicted secondary structures in manganese superoxide dismutase appear to be very similar to those reported for iron superoxide dismutase, suggesting similar three‐dimensional structures. Making use of the known three‐dimensional structure of the Fe enzyme, the Mn ligands are predicted.

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Section: Conserved Sequence Elements Upstream Of the M N Superoxide Dmentioning

confidence: 99%

Section: Conserved Sequence Elements Upstream Of the M N Superoxide Dmentioning

confidence: 99%

Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron‐sulphur protein

Marres¹,

Loon

Oudshoorn³

et al. 1985

European Journal of Biochemistry

126

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“…Since respiratory function is not required under fermentative conditions, many genes coding for mitochondrial proteins are subject to carbon catabolite repression. Thus, genes coding for components of the respiratory chain, like CYC1 (Guarente et al 1984) and QCR8 (DeWinde and Grivell 1992) are repressed when the cells are grown on glucose and transcription is induced roughly ten fold when the cells are grown on a non-fermentable carbon source. The main transcriptional regulator of this induction is thought to be the heterotrimeric transcription-activation complex HAP2/3/4.…”

Section: Introductionmentioning

confidence: 99%

Sequence of the HAP3 transcription factor of Kluyveromyces lactis predicts the presence of a novel 4-cysteine zinc-finger motif

Mulder¹,

Scholten²,

Boer³

et al. 1994

Molec. Gen. Genet.

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Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Abstract The Kluyveromyces lactis homologue of the Saecharomyces cerevisiae HAP3 gene was isolated by functional complementation of the respiratorydeficient phenotype of the S. cerevisiae hap3::HIS4 strain SHY40. The K1HAP3 gene encodes a protein of 205 amino acids, of which the central B-domain of 90 residues is highly homologous to HAP3 counterparts of S. cerevisiae and higher eukaryotes. The protein contains a novel 4-cysteine zinc-finger motif and we propose by analogy that all other homologous HAP3 proteins contain the same motif, with the position containing the third cysteine being occupied by a serine residue. In contrast to the situation in S. cerevisiae, disruption of the K1HAP3 gene in K. lactis does not result in a respiratory-deficient phenotype and the growth of the null strain is indistinguishable from wild type. There is also no effect on the expression of the carbon source-regulated KICYC1 gene, suggesting either a different role for the HAP2/3/4 complex, or the existence of a different mechanism of carbon source regulation. Sequence verification of the S. cerevisiae HAP3 locus reveals that, just as in K. lactis, a long open reading frame (ORF) is present upstream of the HAP3 gene. These highly homologous ORFs are predicted to have at least eight membrane-spanning fragments, but do not show significant homology to any known sequence present in databases. The ScORFX gene is transcribed in the opposite direction to ScHAP3, but, in contrast to an earlier report by Hahn et al. (1988), the transcripts of the two genes do not overlap. The model proposed by these authors, in which the ScHAP3 gene is regulated by an anti-sense non-coding mRNA, is therefore not correct.

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“…In vivo, there are two salient differences in the activity of UAS1B versus CYC7. The former site responds well to HAP1 and gives rise to glucose-repressed transcription that is higher in lactate medium than in glucose medium (11), while the latter site responds poorly and gives rise to a level of transcription that is actually lower in lactate than in glucose (12). The HAP1 response to carbon at CYC7 is counterbalanced by a second element in the CYC7 promoter that is HAPi-independent and gives rise to induction in lactate (12 …”

Section: Fig 1 Functional Domains Of Hap1mentioning

confidence: 94%

Internal deletions in the yeast transcriptional activator HAP1 have opposite effects at two sequence elements

1990

Trends in Genetics

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In this report we study the effects of internal deletions ofthe yeast transcriptional activator HAP1 (CYP1) on activity at two dissimilar DNA binding sites, upstream activation sequence 1 (UAS1) ofCYCI (iso-l-cytochrome c) and CYC7 (iso-2-cytochrome c). These deletions remove up to 1061 amino acids of the 1483-residue protein and bring the carboxylterminal acidic activation domain closer to the amino-terminal DNA-binding domain. Surprisingly, the deletions have opposite effects at the two sites; activity at UAS1 increases with deletion size, while activity at CYC7 decreases. The mutant with the largest deletion, mini-HAPi, has no measurable activit at CYC7 but binds normally to the site in vitro. In contrast, a protein with the DNA-binding domain of HAP1 fused to the acidic activation domain of GALA is active at both UAS1 and CYC7. These findings are discussed in the context oftwo models that suggest how the DNA sequence can alter the activity of the bound HAP1. In a separate experiment, we generate a mutation in the DNA-binding domain of HAP1 that requires the addition of zinc for binding to either UAS1 or CYC7 in vitro. This rinding shows that a zinc finger anchors DNA binding to both types of HAP1 sites.

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Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae

Cited by 486 publications

References 18 publications

Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron‐sulphur protein

Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron‐sulphur protein

Sequence of the HAP3 transcription factor of Kluyveromyces lactis predicts the presence of a novel 4-cysteine zinc-finger motif

Internal deletions in the yeast transcriptional activator HAP1 have opposite effects at two sequence elements

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