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  • 1
    Electronic Resource
    Electronic Resource
    A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A gene (VRP1) encoding a novel proline-rich protein (verprolin) has been isolated from the yeast Saccharomyces cerevisiae as a result of its hybridization to a chick vinculin cDNA probe. The deduced protein sequence contains 24% proline residues present as proline-rich motifs throughout the verprolin sequence. Several of these motifs resemble recently identified sequences shown to bind Src homology 3 (SH3) domains in vitro. Replacement of the wild-type VRP1 allele with a mutant allele results in strains that grow slower than wild-type strains and are temperature sensitive. The vrp1 mutants are impaired in both cell shape and size and display aberrant chitin and actin localization. We propose that verprolin is involved in the maintenance of the yeast actin cytoskeleton, through interactions with other proteins, possibly containing SH3 domains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb00930.x
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  • 2
    Electronic Resource
    Electronic Resource
    The yeast type II myosin heavy chain: Analysis of its predicted polypeptide sequence (1991)
    Springer
    Journal of muscle research and cell motility 12 (1991), S. 61-68 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We have completed the nucleotide sequence of the yeastMYO1 gene and deduced its amino acid sequence. The gene is 5553 bp long and contains no introns. Analysis of the sequence, as well as its comparison with other myosins, demonstrate that the yeast protein is a type II myosin heavy chain with characteristic head and tail regions. The latter domain contains six proline residues in two clusters of three, at approximately two thirds from the start of the gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01781175
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The effect of novobiocin on yeast topoisomerase type II (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 256-260 
    Details
    ISSN: 1617-4623
    Keywords: Topoisomerase II ; Affinity-chromatography ; Novobiocin ; Novobiocin-sepharose ; Novobiocin-resistant mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Low concentrations of novobiocin are toxic to permeable yeast cells, but do not inhibit type II topoisomerase activity. Furthermore, the enzyme does not bind specifically to novobiocin-Sepharose. These observations are in agreement with genetical analyses. Mutations at a single locus that confer novobiocin resistance and temperature sensitivity exhibit a similar phenotype to cells treated with novobiocin, but are not topoisomerase II mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00260491
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The omnipotent suppressor SUP45 affects nucleic acid metabolism and mitochondrial structure (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 6 (1990), S. 441-450 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; novobiocin-resistance ; SUP45 ; nucleic acid synthesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Yeast (Saccharomyces cerevisiae) strains sensitive to a variety drugs were used to select for novobiocin-resistant mutants that were simultaneously temperature-sensitive. The mutants remained as sensitive as the parent strains to a wide range of drugs other than novobiocin, and did not exhibit any suppression of suppressible auxotrophic markers. At the non-permissive temperature, the mutant cells arrested mainly as unbudded cells, and were instantly defective in DNA and RNA synthesis, but not protein synthesis. The cloned wild-type gene was identified as SUP45, which has been previously implicated in the translation process. Our results suggest that SUP45 may have a function in addition to, or different from, the one that has been assigned to it previously.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320060509
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    Paper (German National Licenses)
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