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Published June 1989 | public
Journal Article

A DNA binding protein that recognizes oligo(dA)•oligo(dT) tracts


Oligo(dA)•oligo(dT) tracts are common intergenic sequences in many organisms. In the yeast Saccharomyces cerevisiae, these sequences have been shown to influence transcription of adjacent genes. We have purified an oligo(dA)•oligo(dT)‐binding protein from S. cerevisiae and cloned its gene. This protein, which has been named datin, requires at least 9‐11 bp of oligo(dA)•oligo(dT) DNA for high affinity binding. The gene for datin (the DAT gene) encodes a 248‐residue protein which contains a number of repeated sequence motifs. Datin purified from yeast corresponds to the N‐terminal half of the DAT gene product. Null mutants in the DAT gene are viable but phenotypically distinguishable from congenic wild‐type strains. We discuss unusual structural features and biochemical properties of datin in relation to its possible functions.

Additional Information

© 1989 European Molecular Biology Organization. Received on February 21, 1989. We thank Kim Amdt and Gerald Fink for the dA•dT-CYC1-lacZ plasmid and for communicating their unpublished results, Richard Young for the yeast EMBL3A DNA library and William Lane for amino acid sequence analysis. We thank John McGrath for assistance with the computer analysis, Daniel Finley and Mark Hochstrasser for comments on the manuscript, and are indebted to them and other members of the laboratory for helpful discussions and advice throughout this work. We also thank Barbara Doran for secretarial assistance. The work was supported by grants to A.V. from the National Institutes of Health (CA43309 and GM33401), and by a postdoctoral fellowship to E.W. from the National Institutes of Health (GM10830).

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