Analysis of the in vivo interaction between a basic repressor and an acidic activator.
The artificial basic repressor SSB24 represses transcription of a reporter construct activated by GCN4. We show that the positively charged SSB24 and the negatively charged acidic activator GCN4 interact in vitro and in vivo. However, deleting the interaction domain from the GCN4 activator does not result in loss of repression by SSB24. Similarly, transcription activated by the holoenzyme component SRB2 is repressed, although SSB24 and SRB2 do not interact. Repression by SSB24 therefore does not depend on the observed protein-protein interaction between SSB24 and GCN4.
Wellhausen
A
A
Max-Delbrück-Laboratorium in der Max-Planck-Gesellschaft, Köln, Germany.
Lehming
N
N
D000143:Acids / Q000378:metabolism; D000468:Alkalies / Q000378:metabolism; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000378:metabolism*; D005786:Gene Expression Regulation; D056892:Mediator Complex; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D011994:Recombinant Proteins; D012097:Repressor Proteins / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D017384:Sequence Deletion; D015534:Trans-Activators / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism
D000143:Acids; D000468:Alkalies; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D056892:Mediator Complex; D011994:Recombinant Proteins; D012097:Repressor Proteins; C074748:SRB2 protein, S cerevisiae; C120369:SSB24 protein, recombinant; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D014452:Ubiquitins; D011494:Protein Kinases