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  • Chromosome III  (1)
  • Group II intron  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 223 (1990), S. 249-257 
    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
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  • 2
    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
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