Residues in the WD repeats of Tup1 required for interaction with alpha2.
The yeast transcriptional repressor Tup1 contains seven WD repeats which interact with the DNA-binding protein alpha2. We have identified mutations in Tup1 that disrupt this interaction. The positions of the amino acids changed by these mutations are consistent with Tup1 being folded into a seven-bladed propeller like that formed by another WD repeat-containing protein, the beta subunit of the heterotrimeric G protein used in signal transduction. Our results also indicate that the interaction between Tup1 and alpha2 resembles the interaction between Gbeta and G alpha, suggesting that a similar structural interface is formed by WD repeat proteins that are used in both transcriptional regulation and signal transduction.
Komachi
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K
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0414, USA.
Johnson
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AD
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D018398:Homeodomain Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D017354:Point Mutation; D011485:Protein Binding; D017510:Protein Folding; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic / Q000235:genetics; D014364:Tryptophan / Q000378:metabolism*
D005656:Fungal Proteins; D018398:Homeodomain Proteins; C062928:MATA2 protein, S cerevisiae; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; C066502:TUP1 protein, S cerevisiae; D001224:Aspartic Acid; D014364:Tryptophan