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  • 1
    Electronic Resource
    Electronic Resource
    Tyrosinase exacerbates dopamine toxicity but is not genetically associated with Parkinson's disease (2005)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 93 (2005), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Tyrosinase is a key enzyme in the synthesis of melanin in skin and hair and has also been proposed to contribute to the formation of neuromelanin (NM). The presence of NM, which is biochemically similar to melanin in peripheral tissues, identifies groups of neurons susceptible in Parkinson's disease (PD). Whether tyrosinase is beneficial or detrimental to neurons is unclear; whilst the enzyme activity of tyrosinase generates dopamine-quinones and other oxidizing compounds, NM may form a sink for such radical species. In the present study, we demonstrated that tyrosinase is expressed at low levels in the human brain. We found that mRNA, protein and enzyme activity are all present but at barely detectable levels. In cell culture systems, expression of tyrosinase increases neuronal susceptibility to oxidizing conditions, including dopamine itself. We related these in vitro observations to the human disease by assessing whether there was any genetic association between the gene encoding tyrosinase and idiopathic PD. We found neither genotypic or haplotypic association with three polymorphic markers of the gene. This argues against a strong genetic association between tyrosinase and PD, although the observed contribution to cellular toxicity suggests that a biochemical association is likely.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2005.03019.x
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  • 2
    Electronic Resource
    Electronic Resource
    Plastid photodamage and Cab gene expression in barley leaves (2000)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 109 (2000), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effects of norflurazon (NF) and amitrole (AM), two bleaching herbicides which inhibit carotenogenesis, were compared in leaves of 7-day-old barley (Hordeum vulgare L. cv Express) plants grown in damaging light. The herbicide effects were analysed with respect to chloroplast organization, photosynthetic functionality and nuclear photodependent expression of the Lhcb1 gene, which codes for the Lhcb1 light-harvesting chlorophyll a/b binding protein of photosystem II. Both herbicides caused dramatic photooxidation of organelles, which were photosynthetically unfunctional. Plastids of NF-treated plants lacked thylakoids and pigments. Plastids of AM-treated plants had some strikingly altered membranes and contained only very small quantities of chlorophylls. Despite the presence of severely photodamaged plastids, cells of AM-treated leaves contained high levels of Lhcb1 transcript. This transcript, on the contrary, was completely absent in the cells of NF-treated plants. These findings suggest that in order to block expression of nuclear genes coding for plastid-resident proteins, photodamage leading to the complete dismantling of thylakoids and to the total absence of any form of photosynthetic pigment is required.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2000.100108.x
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of the mitochondrial split gene coding for cytochrome oxidase subunit I in S. cerevisiae: RNA splicing pathway (1986)
    Springer
    Current genetics 11 (1986), S. 55-63 
    Details
    ISSN: 1432-0983
    Keywords: RNA splicing ; cox1 gene ; S. cerevisiae ; Mosaic genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have studied the splicing pathway leading to the synthesis of cytochrome oxidase subunit I (COX I) mRNA, by analysing the transcription pattern of several oxi3 − splicing deficient mutants located in the first four introns of the gene. The four introns contain long open reading frames (ORFs) in phase with the upstream exons. All the mutations block the excision of the mutated intervening sequence (IVS) from the pre-mRNA, and accumulate characteristic novel polypeptides of sizes which could correspond to the translation products of the intron's ORE Most of the mutations do not affect the splicing of the following intervening sequences; only in the case of mutations in the all intron is a polar effect observed on the splicing of the second intron, aI2. Our results indicate that the splicing of these two intervening sequences which both belong to the class II of introns described by Michel et al. (1982), is controlled by the activity of the maturases encoded by their respective ORFs and that the translation of the aI2 maturase depends on the previous excision of all IVS. (Moreover, the aI1 maturase, which accumulates in some mutants, can efficiently splice aI2 IVS when the translation of the latter's proper maturase cannot occur).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00389426
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  • 4
    Electronic Resource
    Electronic Resource
    A controversy concerning the structure of the mitochondrial genome of a yeast petite mutant: resolution by sequence analysis (1989)
    Springer
    Current genetics 15 (1989), S. 291-293 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; oxi3 gene ; Petite genome ; Frameshift mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Sequence analysis was used to define the repeat unit that constitutes the mitochondrial genome of a petite (rho −) mutant of the yeast Saccharomyces cerevisiae. This mutant has retained and amplified in tandem a 2,547 by segment encompassing the second exon of the oxi3 gene excised from wild-type mtDNA between two direct repeats of 11 nucleotides. The identity of the mtDNA segment retained in this petite has recently been questioned (van der Veen et al., 1988). The results presented here confirm the identity of this mtDNA segment to be that determined previously by restriction mapping (Carignani et al., 1983).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447045
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  • 5
    Electronic Resource
    Electronic Resource
    A controversy concerning the structure of the mitochondrial genome of a yeast petite mutant: resolution by sequence analysis (1989)
    Springer
    Current genetics 15 (1989), S. 293-294 
    Details
    ISSN: 1432-0983
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447046
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  • 6
    Electronic Resource
    Electronic Resource
    The photosystem II subunit CP29 can be phosphorylated in both C3 and C4 plants as suggested by sequence analysis (1998)
    Springer
    Plant molecular biology 36 (1998), S. 11-22 
    Details
    ISSN: 1573-5028
    Keywords: chlorophyll a/b protein ; CP29 ; Phosphorylation ; Photosystem II ; cold stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The CP29 subunit of Photosystem II is reversibly phosphorylated in Zea mays upon exposure to high light in the cold (Bergantino et al., J Biol Chem 270 (1995) 8474–8481). This phenomenon was previously proposed to be restricted to C4 plants. We present the complete sequence of the CP29 protein, deduced from a maize Lhcb4 cDNA clone, and its comparison with the previously known Lhcb4 sequences of two C3 plants: Hordeum vulgare and Arabidopsis thaliana. Despite the relatively low degree of homology in their amino-terminal region, i.e. the part of the molecule which is phosphorylated in maize, the three polypeptides conserve consensus sequences for the site of phosphorylation. We proved by immunoblotting and 33P-labelling that the same post-translational modification occurs in barley. Being thus common to C3 and C4 plant species, the phosphorylation of this minor antenna complex of Photosystem II appears now as a widespread phenomenon, possibly part of the phosphorylation cascade which signals the redox status of the plastoquinone to the nuclear transcription apparatus. Arabidopsis plants do not show phosphorylation of CP29 in the same conditions, but other low-molecular-weight phosphoproteins, whose role need to be elucidated, become evident.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005904527408
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  • 7
    Electronic Resource
    Electronic Resource
    Antibodies against a fused gene product identify the protein encoded by a group 11 yeast mitochondrial intron (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 249-257 
    Details
    ISSN: 1617-4623
    Keywords: Antibody ; Hybrid protein ; Group II intron ; Maturase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the mitochondrial genome of Saccharomyces cerevisiae, introns all and aI2 of the gene encoding the COX1 subunit are the only group 11 introns with open reading frames (ORFs); these can be translated into two homologous proteins, the maturase aI1 and aI2. These proteins are structurally related to viral reverse transcriptases and have been shown genetically to be involved in pre-mRNA splicing and in the deletion of introns from mitochondrial DNA. To identify these mitochondrial proteins and study their properties more directly, we raised antibodies against a part of the intron aI2 ORF translation product. For this purpose, we constructed series of fusion genes, by joining parts of the genes for protein A or lacZ to different portions of the intron aI2. These were expressed in Escherichia coli as hybrid polypeptides, which were used for the production and identification of specific antibodies against the yeast mitochondrial protein. The antibodies recognized the 57 kDa protein (maturase aI2) that accumulates in two yeast mutants deficient in the splicing of a12. This protein corresponds to the translation product of the 3′ part of intron aI2 and accumulates unaltered in the two cis-acting mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00265061
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  • 8
    Electronic Resource
    Electronic Resource
    A putative serine/threonine protein kinase gene on chromosome III of Saccharomyces cerevisiae (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 71-77 
    Details
    ISSN: 0749-503X
    Keywords: Protein kinase ; chromosome III ; yeast ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have sequenced a gene on chromosome III of Saccharomyces cerevisiae which codes for a putative serine/threonine protein kinase of 726 amino acids (calculated molecular weight 82 kDa). We have called this gene KIN82. The amino acid sequence of KIN82 is most similar to the cyclic nucleotide-dependent protein kinase subfamily and the protein kinase C subfamily. Gene disruption of KIN82 did not produce any phenotype when tested under a variety of conditons. Reduced stringency hybridizations revealed the presence of another genomic sequence with high homology to the carboxy-terminal catalytic domain of KIN82.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320080108
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  • 9
    Electronic Resource
    Electronic Resource
    The sequence of a 6·3 kb segment of yeast chromosome III reveals an open reading frame coding for a putative mismatch binding protein (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 981-988 
    Details
    ISSN: 0749-503X
    Keywords: Chromosome III ; genome sequencing ; mismatch repair ; post-meiotic segregation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence of a 6·3 kb segment of DNA mapping near the end of the right arm of chromosome III of Saccharomyces cerevisiae. The sequence reveals a major open reading frame coding for a putative protein of 1047 amino acids with a striking similarity to the bacterial proteins involved in recognition of mismatched DNA base pairs. This is particularly interesting as the existence of a yeast mismatch repair system similar to that of bacteria has been postulated for some years, but a yeast protein homologous to the bacterial mismatch binding protein had not been identified.The results of a comparison of the putative yeast mismatch binding protein with the bacterial mismatch binding proteins and with two cognate mammalian sequences, support the idea that a similar mismatch repair system may be present also in mammalian cells. The possibility that all of these proteins may have evolved from a common ancestral gene is also discussed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070910
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