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  • 1
    Electronic Resource
    Electronic Resource
    Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases (1999)
    Springer
    Current genetics 35 (1999), S. 609-617 
    Details
    ISSN: 1432-0983
    Keywords: Key words Cysteine uptake ; Amino-acid permeases ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Uptake by Saccharomyces cerevisiae of the sulphur-containing amino acid L-cysteine was found to be non-saturable under various conditions, and uptake kinetics suggested the existence of two or more transport systems in addition to the general amino-acid permease, Gap1p. Overexpression studies identified BAP2, BAP3, AGP1 and GNP1 as genes encoding transporters of cysteine. Uptake studies with disruption mutants confirmed this, and identified two additional genes for transporters of cysteine, TAT1 and TAT2, both very homologous to BAP2, BAP3, AGP1 and GNP1. While Gap1p and Agp1p appear to be the main cysteine transporters on the non-repressing nitrogen source proline, Bap2p, Bap3p, Tat1p, Tat2p, Agp1p and Gnp1p are all important for cysteine uptake on ammonium-based medium. Furthermore, whereas Bap2p, Bap3p, Tat1p and Tat2p seem most important under amino acid-rich conditions, Agp1p contributes significantly when only ammonium is present, and Gnp1p only contributes under the latter condition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050459
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  • 2
    Electronic Resource
    Electronic Resource
    Mutational analysis of assembly and function of the iron-sulfur protein of the cytochromebc 1 complex inSaccharomyces cerevisiae (1993)
    Springer
    Journal of bioenergetics and biomembranes 25 (1993), S. 245-257 
    Details
    ISSN: 1573-6881
    Keywords: Rieske iron-sulfur protein, RIP1 ; Saccharomyces cerevisiae ; mitochondria ; bc 1 complex ; QCR9 ; iron-sulfur cluster, mitochondrial targeting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The iron-sulfur protein of the cytochromebc 1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochromec 1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochromeb-566 heme group. In order to catalyze this divergent transfer of two reducing equivalents from ubiquinol, the iron-sulfur protein must be structurally integrated into the cytochromebc 1 complex in a manner which facilitates electron transfer from the iron-sulfur cluster to cytochromec 1 and generates a strongly reducing ubisemiquinone anion radical which is proximal to theb-566 heme group. This radical must also be sequestered from spurious reactivities with oxygen and other high-potential oxidants. Experimental approaches are described which are aimed at understanding how the iron-sulfur protein is inserted into center P, and how the iron-sulfur cluster is inserted into the apoprotein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762586
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  • 3
    Electronic Resource
    Electronic Resource
    GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1121-1130 
    Details
    ISSN: 0749-503X
    Keywords: Mitochondrial glycerol 3-phosphate dehydrogenase ; glycerol utilization ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A gut2 mutant of Saccharomyces cerevisiae is deficient in the mitochondrial glycerol 3-phosphate dehydrogenase and hence cannot utilize glycerol. Upon transformation of a gut2 mutant strain with a low-copy yeast genomic library, hybrid plasmids were isolated which complemented the gut2 mutation. The nucleotide sequence of a 3·2 kb PstI-XhoI fragment complementing a gut2 mutant strain is presented. The fragment reveals an open reading frame (ORF) encoding a polypeptide with a predicted molecular weight of 68·8 kDa. Disruption of the ORF leads to a glycerol non-utilizing phenotype. A putative flavin-binding domain, located at the amino terminus, was identified by comparison with the amino acid sequences of other flavoproteins. The cloned gene has been mapped both physically and genetically to the left arm of chromosome IX, where the original gut2 mutation also maps. We conclude that the presented ORF is the GUT2 gene and propose that it is the structural gene for the mitochondrial glycerol 3-phosphate dehydrogenase.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091013
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  • 4
    Electronic Resource
    Electronic Resource
    II. Yeast sequencing reports. The sequence of a 32 420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. S47 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; yeast ; chromosome II ; RIF1 ; DPB3 ; MRP-L27 ; SNF5 ; SEC61-homolog ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The sequence of a 32 420 bp segment of Saccharomyces cerevisiae chromosome II has been deduced. The sequence data revealed 19 potential new genes covering 83·5% of the sequence. Four genes had already been cloned and sequenced: part of RIF1, DPB3, MRP-L27 and SNF5. Besides these four genes, 15 open reading frames (ORFs) of at least 100 amino acids encoding potential new genes were identified. Two of these ORFs are overlapping and a third is located within another ORF.The putative gene product of ORF YBR2039 was homologous to the group of uncoupling proteins involved in the mitochondrial energy transfer system. We propose a remapping of the MRP-L27 gene encoding the mitoribosomal protein YmL27 as it previously has been mapped on chromosome X. The ORF YBR2020 has a strong homology with a 31·9% identity in a 473 amino acid region to the yeast gene SEC61, suggesting that YBR2020 is a new gene encoding a protein involved in translocation of proteins in the yeast cell. Six of the potential genes do not exhibit any significant homology to previously sequenced genes as predicted in the Fast A analysis. The sequence has been deposited in the EMBL data library under Accession Number X76053.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100007
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  • 5
    Electronic Resource
    Electronic Resource
    Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 85-90 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; genome sequencing ; chromosome IV ; DOA4 ; UBC5 ; UBC3 ; DNA52 ; ribosomal protein gene ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have sequenced a region containing 32.5 kb of the right arm of chromosome IV of Saccharomyces cerevisiae. Twenty open reading frames (ORFs) greater than 100 amino acids could be identified in this region. Six ORFs correspond to known yeast genes, including DOA4, UBC5 and UBC3, the gene products of which are involved in ubiquitin metabolism. UBC5 is preceded by the two tRNA genes tRNA-Arg2 and tRNA-Asp. Six genes were discovered with homologies to non-yeast genes or with homologies to other yeast ORFs. One of these could be identified as ribosomal protein gene RPS13. The putative function of eight ORFs remains unclear because comparison to different DNA or protein databases revealed no significant patterns. The sequence from cosmid 2F21 was obtained entirely by a combined subcloning and walking primer strategy, and has been deposited in the EMBL data library under Accession Number X84162.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Review: Biosynthesis and function of yeast vacuolar proteases (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1-16 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; lysosome ; sorting ; proteolytic activation ; endocytosis autophagocytosis ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The yeast vacuole, which is equivalent to the lysosome of higher eukaryotes, is one of the best characterized degradative organelles. This review describes the biosynthesis and function of yeast vacuolar proteases. Most of these enzymes are delivered to the vacuole via the early compartments of the secretory pathway and the endosome, while one of them is directly imported from the cytoplasm. The proteases are synthesized as precursors which undergo many post-translational modifications before the final active form is generated. Proteolytic activation by removal of propeptides is performed by proteinase A and/or proteinase B in an intricate cascade-like fashion. Recent developments in the analysis of the functions of vacuolar proteolysis are described. Substrates of the vacuolar proteases are mostly imported via endocytosis or autophagocytosis, and vacuolar proteolysis appears to be mainly important under nutritional stress conditions and sporulation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Mutations in five loci affecting GAP1-independent uptake of neutral amino acids in yeast (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 103-114 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; amino acid uptake ; ssy mutants ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In order to identify genes involved in uptake of isoleucine, leucine and valine in Saccharomyces cerevisiae we isolated mutants that, on a complex medium, were sensitive to an inhibitor of the biosynthesis of the branched-chain amino acids. Mutants that in a secondary screen showed reduced uptake of isoleucine, leucine and valine when growing in synthetic complete medium were further characterized. Genetic analysis identified five loci, named ssy1 through ssy5. ssy2 corresponds to the previously characterized bap1 mutation, which we recently have found to be allelic to stp1. ssy1, ssy3 and ssy5 exhibit a reduced uptake of phenylalanine, methionine and threonine, as well. Furthermore, they are resistant to several neutral amino acid analogs. ssy4 only affects uptake of few neutral amino acids and is as sensitive as the wild type to the amino acid analogs tested. It was previously found that a C-terminal truncation of 29 codons of BAP2, which encodes a branched-chain amino acid permease, results in increased uptake of the branched-chain amino acids. We find epistasis of the C-terminally truncated BAP2 gene over the ssy4 mutation, while the other ssy mutations are epistatic over the truncated BAP2 gene. SSY1, SSY3 and SSY5 were cloned from a low-copy genomic library by complementation of the mutants. The SSY3 gene and the SSY5 gene show no significant homology to any sequence in the databases. SSY1 is a member of the major family of genes encoding amino acid permeases in yeast. We discuss possible roles of Ssy1p in amino acid uptake. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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