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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Overproduced fusions of Sup35 or its prion domain with green fluorescent protein (GFP) have previously been shown to form frequent dots in [PSI+] cells. Rare foci seen in [psi−] cells were hypothesized to indicate the de novo induction of [PSI+] caused by the overproduced prion domain. Here, we describe novel ring-type aggregates that also appear in [psi−] cultures upon Sup35 overproduction and show directly that dot and ring aggregates only appear in cells that have become [PSI+]. The formation of either type of aggregate requires [PIN+], an element needed for the induction of [PSI+]. Although aggregates are visible predominantly in stationary-phase cultures, [PSI+] induction starts in exponential phase, suggesting that much smaller aggregates can also propagate [PSI+]. Such small aggregates are probably present in [PSI+] cells and, upon Sup35–GFP overproduction, facilitate the frequent formation of dot aggregates, but only the occasional appearance of ring aggregates. In contrast, rings are very frequent when [PSI+] cultures, including those lacking [PIN+], are grown in the presence of GuHCl or excess Hsp104 while overexpressing Sup35–GFP. Thus, intermediates formed during [PSI+] curing seem to facilitate ring formation. Surprisingly, GuHCl and excess Hsp104, which are known to promote loss of [PSI+], did not prevent the de novo induction of [PSI+] by excess Sup35 in [psi−][PIN+] strains.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Sup35 protein can exist in a non-infectious form or in various infectious forms called [PSI+] prion variants (or prion strains). Each of the different [PSI+] prion variants converts non-infectious Sup35 molecules into that prion variant's infectious form. One definition of a ‘prion domain’ is the minimal fragment of a prion protein that is necessary and sufficient to maintain the prion form. We now demonstrate that the Sup35 N region (residues 1–123), which is frequently referred to as the ‘prion domain’, is insufficient to maintain the weak or strong [PSI +] variants per se, but appears to maintain them in an ‘undifferentiated’[PSI+] state that can differentiate into weak or strong [PSI+] variants when transferred to the full-length Sup35 protein. In contrast, Sup35 residues 1–137 are necessary and sufficient to faithfully maintain weak or strong [PSI+] variants. This implicates Sup35 residues 124–137 in the variant-specific maintenance of the weak or strong [PSI+] forms. Structure predictions indicate that the residues in the 124–137 region form an α-helix and that the 1–123 region may have β structure. In view of these findings, we discuss a plausible molecular basis for the [PSI+] prion variants as well as the inherent difficulties in defining a ‘prion domain’.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature America Inc.
    Nature genetics 23 (1999), S. 8-10 
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] A large number of human genetic diseases result from mutations that cause the premature termination of the synthesis of the protein encoded by the mutant gene. A study by Elisabeth Barton-Davis and colleagues, exploring antibiotic effect on a mouse model of Duchenne muscular dystrophy (DMD) and ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The yeast amber suppressor, SUP5-a, was previously shown to cause the insertion of tyrosine at the sites of UAG nonsense codons. Nucleotide sequencing established that this SUP5-a suppressor specifies a mutant tyrosine transfer RNA (tRNA) which has the anticodon CΨA instead of the ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 410 (2001), S. 161-162 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The recent epidemics of 'mad cow' disease have put the fatal, transmissible spongiform encephalopathies — the so-called prion diseases — firmly in the public eye. It seems likely that the infectious agent in these mammalian diseases is the PrP protein, in the absence of traditional ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 16 (1989), S. 315-321 
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Antisuppressor ; ADE3 ; Translation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in a known yeast gene, ADE3, were shown to act as an antisuppressor, reducing the efficiency of the omnipotent suppressor, sup45-2. The ADE3 locus encodes the trifunctional enzyme C1-tetrahydrofolate synthase, which is required for the biosynthesis of purines, thymidylate, methionine, histidine, pantothenic acid and formylmethionyl-tRNAfmet. The role of this enzyme in translational fidelity had not previously been suspected.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 12 (2005), S. 567-568 
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Many soluble proteins can convert into insoluble amyloid-like fibrils. Such fibrils are also associated with proteins, called prions, that undergo a self-perpetuating change from a soluble to an aggregated form. Conversion of the mammalian PrP prion protein into fibrils is associated with ...
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Chromosoma 105 (1997), S. 444-451 
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The ribosomal RNA (rRNA) genes of most eukaryotic organisms are arranged in one or more tandem arrays, often termed nucleolar organizer regions. The biological implications of this tandem organization are not known. We have tested the requirement for such a chromosomal organization by directly comparing the transcription and processing of rRNA in isogenic strains of Saccharomyces cerevisiae that differ only in the organization of their rRNA genes. Strain L-1489 carries the RDN locus, consisting of 100–150 copies of the rRNA genes in a tandem array on chromosome XII. Strain L-1521 has a complete deletion of the RDN array, but carries many copies of a plasmid that includes a single rRNA gene. While this strain grows reasonably well, the average transcriptional activity of the plasmid genes is substantially less than that of the chromosomal copies. However, there is little difference in the processing of the 35S pre-rRNA to the mature 25S:5.8S and 18S products. Thus, neither a chromosomal location nor a tandem repeat of the rRNA genes is important for the assembly and function of the many protein and RNA molecules necessary for the processing of the rRNA transcripts. We investigated the consequence of a dispersed gene arrangement on nucleolar structure. Immunofluorescence microscopy revealed that in strain L-1521 the yeast fibrillarin, Nop1p, rather than being confined to a defined nucleolus at the edge of the nucleus as it is in cells with the normal arrangement of rRNA genes, is spread throughout the nucleus. This observation implies that each plasmid rRNA gene can serve as a nucleolar organizer. Finally, data from pulse-labeling experiments show that the repression of rRNA transcription due to failure of the secretory pathway is independent of whether the rRNA genes are at the RDN locus on chromosome XII or on plasmids. This result suggests that the regulation of rRNA transcription occurs at the level of soluble factors rather than chromatin structure.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0983
    Keywords: Ribosomes ; Antisuppressor ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The yeast antisuppressor mutation, asu9-1 (Liebman and Cavenagh 1980) was found to cause an alteration in the 40S ribosomal subunit. Two-dimensional polyacrylamide gel electrophoresis patterns of the 40S ribosomal proteins from four different strains bearing the asu9-1 mutation all contained the same extra protein spot which was completely absent in five strains which did not carry the asu9 mutation.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-0983
    Keywords: Key Words Rad6 ; Ubiquitination ; Silencing ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Null mutations in the RAD6/UBC2 gene encoding an E2 ubiquitin-conjugating enzyme cause deficiencies in DNA repair, N-end-rule protein degradation, sporulation and telomeric silencing, and alter the preferred integration positions for Ty1 retrotransposons. Here we selected for mutants of RAD6 that cause a release of telomeric silencing. Some alleles retained nearly wild-type ability for sporulation, DNA repair and the degradation of proteins. Alteration in Ty1 integration-site bias accompanied some of these alleles. The possibility that some mutations specifically affect binding of an unknown protein that works with Rad6 in its silencing role, but is not required for DNA repair or N-end-rule activity, is discussed in terms of the Rad6 crystal structure.
    Type of Medium: Electronic Resource
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