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  • 1
    Electronic Resource
    Electronic Resource
    Purification of yeast histones competent for nucleosome assembly in vitro (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 319-331 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; histones ; nucleosome assembly ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have developed a procedure to purify nucleosomal assembly-competent histones as a mixture of H2A, H2B, H3 and H4 from isolated nuclei of the yeast Saccharomyces cerevisiae with a purity of 70-80%. The mixture contained each of the histone subunits approximately at the equi-molar ratio. Plasmid pBR322 DNA was assembled into nucleosomes with the purified yeast histones in the presence of nucleoplasmin from unfertilized eggs of the frog Xenopus laevis. The efficiency of assembly of yeast histones was comparable to that of core histones purified from HeLa cells. The length of DNA fragment wrapping around a core histone particle and the molar ratio of histone components in an assembled nucleosome particle were estimated to be 150 ± 10 bp long and H2A:H2B:H3:H4 = 1·0:0·9:0·9:1·0, respectively.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100305
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  • 2
    Electronic Resource
    Electronic Resource
    Primary structure of the Saccharomyces cerevisiae GAL7 gene (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 1 (1985), S. 67-77 
    Details
    ISSN: 0749-503X
    Keywords: Galactose metabolism ; regulation ; genefusion ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We present the nucleotide sequence of a 1599-base pair (bp) DNA fragment containing the entire GAL7 gene that encodes galactose-1-phosphate uridyltransferase of Saccharomyces cerevisiae. The deduced peptide was composed of 364 amino acid residues. The expected molecular weight was 42 005 daltons, which agreed with the observed value for the purified enzyme.1 The 3′-end of the GAL7 transcript mapped at a position 82 bp downstream from the UAA termination codon by the S1 nuclease protection experiment. We constructed a GAL7′-lac′Z fusion on various types of yeast plasmid vectors. The fused gene on any type of vector was induced by galactose and repressed by glucose as for the GAL7 gene on the chromosome. The response of GAL7′-lac′Z fusion to gal4Δ and gal80Δ regulatory mutations was also similar to the response of the chromosomal GAL7 gene. By using various deletions in the 5′-flanking region of the gene fusion, we delimited the sequence essential for galactose controlled expression with a 180 bp-fragment of DNA lying 92 bp upstream of the transcription initiation site.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320010108
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