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Mol. Cell. Biol., Oct 1997, 6023-6028, Vol 17, No. 10
Copyright © 1997, American Society for Microbiology

Residues in the WD repeats of Tup1 required for interaction with alpha2

K Komachi and AD Johnson
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0414, USA.

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.


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