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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The non-essential RGD1 gene from Saccharomyces cerevisiae encodes a protein that has been characterized in vitro as a Rho GTPase activating protein (RhoGAP) for the Rho3 and Rho4 proteins. Rgd1p, which displays a conserved FCH–coiled coil–RhoGAP domain organization, showed a patch-like distribution in the cell, including a localization in growing buds. Using a genetic screen, we found that rgd1Δ and vrp1Δ mutations exhibited a synthetic lethality, thus revealing an interaction between these genes. The VRP1 product is an actin and myosin interacting protein involved in polarized growth. Using mutant forms of both Rho3 and Rho4 proteins, we provide evidence for the involvement of these two GTPases in RGD1–VRP1 co-lethality. In addition, these results strongly argue in favour of Rho3p and Rho4p being the targets of Rgd1p RhoGAP activity in vivo. Genetic relationships between either VRP1 or RGD1 and actin cytoskeleton-linked genes were also studied. These and other well-established data support the idea that Vrp1, Las17, Rvs167 proteins belong to the same complex. This protein structure might act with myosins in various actin cytoskeleton-based activities, in co-operation with a Rho3p/Rho4p signalling pathway that is negatively regulated by Rgd1p GAP activity.
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  • 2
    ISSN: 0749-503X
    Keywords: multicopy suppression ; RVS167 ; RVS161 ; actin cytoskeleton ; budding pattern ; membrane protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The rvs161 and rvs167 mutant cells exhibit several identical phenotypes including sensitivity to several different growth conditions and morphological defects such as alteration of the actin cytoskeleton and budding patterns. The selection of genes that, when overexpressed, are able to suppress the reduced viability upon carbon starvation of the rvs167 mutant strain, has allowed the cloning of the SUR7 gene (Accession Number Z46729x11).We showed that the suppressive ability of the overexpressed SUR7 gene concerns all the rvs167 phenotypes. However, this suppression is only partial since the rvs167-suppressed strain is not of wild-type phenotype. Moreover, SUR7 is also able to suppress partially the phenotypes exhibited by the rvs161 and rvs167 rvs161 mutant strains.The SUR7 gene encodes a putative integral membrane protein with four transmembrane domains. Furthermore, sequence comparisons revealed that Sur7p and two other proteins, Ynl194p and Ydl222p, present significant sequence and structural similarities.Taken together, these results strongly suggest that the Rvs161 and Rvs167 proteins act together in relation with Sur7p. Moreover, the putative transmembranous character of Sur7p suggests a membrane localization of the Rvs function, a localization which is consistent with the different rvs phenotypes and the actin-Rvs167p interaction. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II sequencing ; serine-hydroxymethyl-transferase ; RIB5 ; GAP ; GTP binding protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report here the sequence of a 19,482 bp DNA segment of chromosome II of Saccharomyces cerevisiae. The fragment contains 16 open reading frames (ORFs) covering 74% of the sequence. Four predicted products present homology with known proteins. The ORF YBR1732 exhibits a strong homology to serine hydroxymethyl transferase; the best score is 53·1% identity in 458 amino acids overlap with the serine hydroxymethyl transferase from rabbit liver. YBR1724, which shows homology with riboflavin synthase of Bacillus subtilis, is probably the RIB5 gene implied in riboflavine synthesis and mapped in this region. YBR1733 is homologous to rab protein and YBR1728 is presumably a GTPase activating protein.
    Additional Material: 5 Ill.
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  • 4
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; HSP26 ; SEC18 ; UBC4 ; tRNAarg ; tRNAasp ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a 31 352 bp fragment from chromosome II of Saccharomyces cerevisiae has been determined and analysed. The fragment originates from the right arm of chromosome II, located between the GAL7,10,1 and the PHO3,5 loci, at a distance of about 130 kb from the centromere. The sequence contains a tRNA tandem repeat and 17 open reading frames (ORFs) larger than 100 amino acids. One of them extends into adjacent DNA and is incomplete. The two tRNA genes, coding for a tRNAasp and a tRNAarg, and three of the ORFs, had been sequenced previously, i.e. HSP26, SEC18, and UBC4. Four other ORFs showed similarity with yeast genes; amino acid transporter genes, the RAD54, SNF2 and STH1 family, the SPS2 gene and the bromodomain of SPT7, respectively. Two showed homology with sequences from other organisms, i.e. with a Plasmodium falciparum gene encoding a surface antigen and with a gene from Saimirine herpes virus respectively. Three ORFs, YBR0726, YBR0735 and YBR0740 are completely contained in YBR0727, YBR0734 and YBR0739 respectively, and thus probably do not represent real genes. Two ORFs, YBR0727 and YBR0745 most likely contain an intron. The sequences have been deposited in the EMBL data library under Accession Number X76294.
    Additional Material: 1 Ill.
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  • 5
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; genome sequencing ; chromosome XIV ; cytochrome c oxidase ; actin ; tyrosine phosphatase ; porin ; nucleolar protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have determined the complete nucleotide sequence of a 44 420 bp DNA fragment from chromosome XIV of Saccharomyces cerevisiae. The sequence data revealed 23 open reading frames (ORFs) larger than 300 bp, covering 73·5% of the sequence. The ORFs N2418, N2441, N2474 and N2480 correspond to previously sequenced S. cerevisiae genes coding respectively for the mitochondrial import protein Mas5, the nucleolar protein Nop2, the outer mitochondrial membrane porin Por1, the cytochrome c oxidase polypeptide VA precursor CoxA and the yeast protein tyrosine phosphatase Msg5. Translation products of three other ORFs N2406, N2411 and N2430 exhibit similarity to previously known S. cerevisiae proteins: the ribosomal protein YL9A, the protein Nca3 involved in the mitochondrial expression of subunits 6 and 8 of the ATP synthase and actin; in addition N2505 presents strong similarity to an ORF of chromosome IX. The predicted protein products of ORFs N2417 and N2403 present similarities with domains from proteins of other organisms: the Candida maltosa cycloheximide-resistance protein, the human interleukin enhancer-binding factor (ILF-2). The 12 remaining ORFs show no significant similarity to known proteins. In addition, we have detected a DNA region very similar to the yeast transposon Ty 1-15 of which insertion has disrupted a tRNAAsp gene. The sequence has been deposited in the GenBank database with the Accession Number U12141.
    Additional Material: 1 Ill.
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  • 6
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II ; DNA sequencing ; dUTPase ; S5 protein ; ARO4 gene ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DNA sequence of a 6794 bp fragment located at about 100 kb from the right telomere of chromosome II from Saccharomyces cerevisiae has been determined. Sequence analysis reveals five open reading frames. One is the ARO4 gene encoding the 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase. Another presents strong homology with the S5 ribosomal protein from bacteria. The open reading frame YBR1705 shows significant homology with dUTPase, suggesting for the first time the existence of such an enzyme in S. cerevisiae.
    Additional Material: 4 Ill.
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  • 7
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
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