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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 1-14 
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; cell cycle ; budding ; spore germination ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cloning and sequencing of RCS1, a Saccharomyces cerevisiae gene whose product seems to be involved in timing the budding event of the cell cycle, is described. A haploid strain in which the 3′-terminal region of the chromosomal copy of the gene has been disrupted produces cells that are, on average, twice the size of cells of the parental strain. The critical size for budding in the mutant is similarly increased, and the disruption mutation is dominant in a diploid heterozygous for the RCS1 gene. Spores from this diploid have a reduced ability to germinate, the effect being more pronounced in the spores carrying the disrupted copy of RCS1. However, disrupted cells recover from α-factor treatment equally as well as wild-type cells.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 875-887 
    ISSN: 0749-503X
    Keywords: Yeast ; Candida albicans ; Secretion ; Gene Cloning ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The SEC18 gene product is required for protein transport at different stages in the Saccharomyces cerevisiae secretory pathway. The homologous SEC18 gene from Candida albicans has been cloned by complementation of a sec18-1 S. cerevisiae thermosensitive mutant using a C. albicans genomic library in YRp7. Sequence analysis of the gene revealed a 2382-bp open reading frame which coded for a protein of 88 926 kDa. By an in vitro transcription-translation coupled reaction of the C. albicans SEC18 gene, a protein of approximately 85 kDa was obtained. Hydrophobicity analysis of the protein did not show any predicted signal sequence nor transmembrane anchor domain. These results and the fact that glycosylation was absent in the protein indicated that C. albicans Sec18p did not enter in the secretory pathway. The alignment of the amino acid sequence revealed that the SEC18 gene from C. albicans was homologous to the SEC18 from S. cerevisiae (50% amino acid identity) and to the gene that coded the N-ethylmaleimide-sensitive factor (NSF) protein (43% amino acid identity). Moreover, the C. albicans Sec18p also showed the putative ATP binding site present in S. cerevisiae Sec18p and in NSF.
    Additional Material: 9 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 1375-1381 
    ISSN: 0749-503X
    Keywords: Candida albicans ; prolyl tRNA synthetase ; CaPRS ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have isolated a 4·0-kb fragment from a genomic library of Candida albicans which contained two open reading frames (ORFs). One of them is homologous to a prolyl-tRNA synthetase that catalyses the charging of a specific tRNA by proline (CaPRS). A deduced sequence of 575 amino acids representing a polypeptide of 66·2 kDa was determined. A FASTA search indicated that the CaPRSp had an overall similarity of 54·4% with the product of a Saccharomyces cerevisiae ORF (YER087) and 43·8% with the prolyl-tRNA synthetase of Escherichia coli (COLIPRO). Consensus Class II aminoacyl-tRNA synthetase sequences were identified by the PROSITE program. CaPRS was localized to chromosome R of the C. albicans genome and CaPRS DNA hybridized to a major RNA transcript of 1·7 kb under all conditions tested. The CaPRS sequence submitted to the EMBL data library is available under Accession Number U86341.© 1997 John Wiley & Sons, Ltd.
    Additional Material: 6 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1535-1548 
    ISSN: 0749-503X
    Keywords: Yarrowia lipolytica ; cell wall ; mycelium ; cDNA ; YWP1 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector λgt11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is solubilized following partial degradation of β-glucan by Zymolyase digestion. The protein is localized in the outer surface on the tip of the growing mycelial cells and is found partially cryptic in sub-apical locations, suggesting that it participates directly in the mycelial wall architecture.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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