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Separation of DNA binding from the transcription-activating function of a eukaryotic regulatory protein.

Science (New York, N.Y.) (1986-02-14)
L Keegan, G Gill, M Ptashne
RÉSUMÉ

The yeast GAL4 protein (881 amino acids) binds to specific DNA sites upstream of target genes and activates transcription. Derivatives of this protein bearing as few as 74 amino terminal residues bind to these sites but fail to activate transcription. When appropriately positioned in front of a gene these derivatives act as repressors. These and related findings support the idea that GAL4 activates transcription by touching other DNA-bound proteins.

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Sigma-Aldrich
GAL4 [(1-147) + VP16 (411-490)] from Saccharomyces cerevisiae human herpesvirus 2, recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Sigma-Aldrich
GAL4 [(1-147) + E1A (121-223)] from Saccharomyces cerevisiae canine adenovirus, recombinant, expressed in E. coli, ≥70% (SDS-PAGE)