The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Loon, A. P. G. M. Van; Groot, Raoul J. de; Haan, M. de; Dekker, A.; Grivell, Leslie A.

doi:10.1002/j.1460-2075.1984.tb01924.x

Cited by 95 publications

(29 citation statements)

References 30 publications

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“…The cells were suspended in buffer A(200), as described by Bram and Kornberg (4), without pepstatin or leupeptin. The suspension was then sonicated for 5 min and centrifuged for 1 (60), an adjacent gene, CDC26 (our unpublished results), and UCR6 encoding subunit VI of mitochondrial ubiquinol-cytochrome c reductase (55). The direction of reading of PH04 is toward the centromere of chromosome VI (28), as deduced from data of three-factor crosses with the PH04C, pho4-1, and metlO alleles (50) and physical mapping of the PH04C and pho4-J mutation sites.…”

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Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae.

Ogawa¹,

Oshima²

1990

Mol. Cell. Biol.

104

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The PH04 gene encodes a positive regulatory factor involved in regulating transcription of various genes in the phosphatase regulon of Saccharomyces cerevisiae. Besides its own coding region, the 1.8-kilobase PH04 transcript contains a coding region for a mitochondrial protein which does not appear to be translated. Four functional domains were found in the PH04 protein, which consists of 312 amino acid (aa) residues as deduced from the open reading frame of PHO4. A gel retardation assay with 0-galactosidase::PH04 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHOS, a gene under the control of PHO4. This region has similarities with the amphipathic helix-loop-helix motif of c-myc protein. Determination of the nucleotide sequences of four PH04C mutant alleles and insertion and deletion analyses of PH04 DNA indicated that a region from aa 163 to 202 is involved in interaction with a negative regulatory factor PH080. Complementation of a pho4 null allele with the modified PH04 DNAs suggested that the N-terminal region (1 to 109 aa), which is rich in acidic aa, is the transcriptional activation domain. The deleterious effects of various PH04 mutations on the constitutive transcription of PH05 in PH04C mutant cells suggested that the region from aa 203 to 227 is involved in oligomerization of the PH04 protein.The repressible acid phosphatase (rAPase; EC 3.1.3.2) in Saccharomyces cerevisiae consists of a major p60 protein, encoded by PHO5, and the minor species p58 and p56, encoded by PHOIO and PHOJl, respectively (38,49). The expressions of these genes are repressed at the transcriptional level by Pi in the medium (19,21). The Pi signals are conveyed through a system composed of at least five gene products, those from PHO2, PHO4, PHO80, PHO81, and PHO85 (33). The PHO85 product is necessary for expression of PHO80 (53), whereas the others are directly involved in the regulatory system (59-61). A recessive mutation at the PHO2, PHO4, or PHO81 locus blocks the derepression of the structural genes of rAPase, whereas a recessive mutation in PHO80 or PHO85 results in constitutive expression of PHO5. Dominant PH04C mutant alleles (formerly named PHO82) cause a constitutive phenotype of rAPase synthesis (50). PHO4 (60) and PHO80 (53) [61].) In high-Pi medium, the PHO80 product, i.e., the negative regulatory factor, interacts directly with the positive factor and prevents transcription of the structural genes of the phosphatase regulon.We report here a dissection of four functional domains of the PH04 protein. The DNA-binding domain is located at the C terminus and has significant similarities with the amphipathic helix-loop-helix (A-HLH) motif of c-myc (29,37). A site for interaction with the negative regulatory factor PHO80 appears to be located in the central region. We * Corresponding author. present evidence for a region necessary for oligomerization of PH04 beside the site for PHO80 interaction. We also suggest that the transcription-activation domain is loc...

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“…There are numerous other AccII sites in other portions of the PH04 DNA (not illustrated). The wavy arrows represent transcripts of 1.8-kb PH04 and 700-base UCR6 (cited from Van Loon et al [55] (Fig. 1A) is sufficient to complement a pho4 mutation, and the PH04 mRNA is 1.8 kilobases (kb) (60).…”

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confidence: 99%

Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae.

Ogawa¹,

Oshima²

1990

Mol. Cell. Biol.

104

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“…In analogy with complex 111 of Neurospora crassa [8,91, we may assume that the bulk of the two core subunits extends into the mitochondria] matrix while, according to their primary structure [lo, 111, a transmembrane location seems unlikely. The 17-kDa subunit is thought to be homologous to the hinge protein of the bovine-heart complex 111 [12,131. This hinge protein can be cross-linked to both cytochrome c1 [14,15] and cytochrome c [14].…”

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Membrane topography of the subunits of ubiquinol – cytochrome‐c oxidoreductase of Saccharomyces cerevisiae

Hemrika

Berden

1990

European Journal of Biochemistry

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The topology of the subunits of ubiquinol–cytochrome‐c oxidoreductase of the yeast Saccharomyces cerevisiae has been determined using a digitonin/proteinase K assay. With this assay we were able selectively to disrupt the mitochondrial membranes and to identify the subunits which became proteinase‐K‐sensitive after disruption of either the outer or both outer and inner membranes. This approach confirmed previous indications for the localization of the core I protein, cytochrome c1, cytochrome b, the FeS protein and the 17‐kDa subunit, while it also provided direct evidence for the site of accessibility to proteinase K of the 14‐kDa and 11‐kDa subunits. The 14‐kDa subunit faces the mitochondrial matrix and the 11‐kDa subunit faces the intermembrane space.

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“…The bovine hinge protein has a unique segment of eight glutamate residues in the amino-terminal region [lo] which is homologous with the yeast 17-kDa subunit of complex III [13]. Therefore, we made an oligonucleotide that encodes the aminoterminal region as a cloning probe as described in section 2.…”

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An extremely acidic amino‐terminal presequence of the precursor for the human mitochondrial hinge protein

Ohta¹,

Gotō²,

Arai³

et al. 1987

FEBS Letters

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Mitochondrialhinge protein is a subunit of ubiquinol-cytochrome-c reductase in the respiratory chain and 'hinges' cytochrome c with cytochrome c,. The protein is encoded in the nuclear genome, synthesized in the cytosol and then imported into the mitochondria.The cDNA of the human hinge protein has been cloned and its nucleotide sequence was determined. The deduced primary structure of the amino-terminal presequence consists of 13 amino acid residues, of which 4 amino acids are acidic and only one is basic. Since the presequences of most other precursors are rich in basic amino acids, this sequence is unique for targeting mitochondria.Expression of the gene was repressed in the presence of a phorbol ester in human promyelocyticleukemia cells (HL-60) and this repression was greater than that of the ADP/ATP translocator. These findings suggest that the hinge protein, the expression of which is well regulated, is imported into mitochondria via a specific pathway.

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The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Cited by 95 publications

References 30 publications

Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae.

Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae.

Membrane topography of the subunits of ubiquinol – cytochrome‐c oxidoreductase of Saccharomyces cerevisiae

An extremely acidic amino‐terminal presequence of the precursor for the human mitochondrial hinge protein

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