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Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae.

Proceedings of the National Academy of Sciences of the United States of America, 01 May 1980, 77(5):2546-2550
https://doi.org/10.1073/pnas.77.5.2546 PMID: 6994099 PMCID: PMC349438

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Abstract 

The complete nucleotide sequence of the actin gene from Saccharomyces cerevisiae has been determined. The coding region is interrupted by a 304-base-pair intervening sequence that is located within the triplet coding for amino acid 4. DNA sequences of the intron-exon junctions are similar to those found in higher eukaryotes and can be aligned such that the intron starts with the dinucleotide 5'-G-T-3' and ends with 5'-A-G-3'. Regions fo homology within the sequences upstream from the initiation codon and those following the termination codon have been detected between the yeast iso-1-cytochrome c gene and the actin gene. As deduced from the nucleotide sequence, yeast actin has 374 amino acid residues. Its primary structure, especially the NH2-terminal third of the protein, is highly conserved during evolution.

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Proc Natl Acad Sci U S A. 1980 May; 77(5): 2546–2550.
PMCID: PMC349438
PMID: 6994099

Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae.

D Gallwitz and I Sures
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Abstract

The complete nucleotide sequence of the actin gene from Saccharomyces cerevisiae has been determined. The coding region is interrupted by a 304-base-pair intervening sequence that is located within the triplet coding for amino acid 4. DNA sequences of the intron-exon junctions are similar to those found in higher eukaryotes and can be aligned such that the intron starts with the dinucleotide 5'-G-T-3' and ends with 5'-A-G-3'. Regions fo homology within the sequences upstream from the initiation codon and those following the termination codon have been detected between the yeast iso-1-cytochrome c gene and the actin gene. As deduced from the nucleotide sequence, yeast actin has 374 amino acid residues. Its primary structure, especially the NH2-terminal third of the protein, is highly conserved during evolution.

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Selected References

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