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At Least Three Subdomains of v-erbA Are Involved in Its Silencing Function

Laboratoire de Biologie Moléculaire et de Génie Génétique Institut de Chimie-B6 Université de Liège B-4000 Sart-Tilman, Belgium
Genetisches Institut (A.B. R.R.) Justus-Liebig-Universität D-35392 Giessen, Germany

Several members of the thyroid hormone receptor (TR) family are able to switch from a transcriptional repressor to a transcriptional activator upon binding of their ligand. The oncogene v-erbA is a variant form of the TR unable to bind hormone and thus acts as a constitutive repressor. We demonstrate, using fusion proteins between the DNA-binding domain of the yeast factor GAL4 and the silencing domains of v-erbA and TRß, that point mutations in three different regions severely affect their repression function. Furthermore, the three regions, each as an inactive fusion protein with the GAL4 DNA-binding domain, restore silencing activity when assembled on the same promoter. These observations define at least three silencing subdomains, SSD1–SSD3, which are involved in the silencing function of v-erbA. We propose a model in which full silencing activity is brought about by the combined interaction of each silencing subdomain with corepressors and/or basal transcription factors.

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