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Efficient transcription of many Saccharomyces cerevisiae genes requires the GAL11 Protein. GAL11 belongs to a class of transcription activator that lacks a DNA-binding domain. Such proteins are thought to activate specific genes by complexing with DNA-bound proteins. To begin to understand the domain tructurefunction relationships of GAL11 we cloned and sequenced a homologue from the yeast Kluyveromyces lactis, KI-GAL11. The two predicted GAL11 proteins show high overall amino acid conservation and an unusual amino acid composition including 18% glutamine, 10% asparagine (S.cerevisiae) or 7% (K.lactis), and 8% proline (K.lactis) or 5% (S.cerevisiae) residues. Both proteins have runs of pure glutamines. Sc-GAL11 has glutamine-alanine runs but in KI-GAL11 the alanines in such runs are replaced by proline and other residues. The primary sequence similarity is reflected in functional similarity since a gall 1 mutation in K.lactis creates phenotypes similar to those seen previously in gall 7-defective S.cerevisiae. In addition, KI-GAL11 complements a ga/f f-defect in S.cerevisiae by partially restoring induction of GAL1 expression, growth on nonfermentable carbon sources, andphosphorylation of GAL4.


Mylin, Larry, et al. (1991). Sequence Conservation in the Saccharomyces and Kluveromyces GAL11 Transcription Acvivators Suggests Functional Domains. Nucleic Acids Research 19(19),5345-5350.

© 1991 Oxford University Press. Original published version available at

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