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The Groucho (Gro)/Transducinlikeenhancer of split (TLE) family of corepressors plays a significant role in the regulation of many cellular processes. Having no intrinsic DNAbinding activity, Gro/TLE interacts with various DNAbound repressor proteins to repress transcription. Gro/TLE possesses a conserved region known as the Qdomain, and this region has been shown to direct the oligomerization of Gro/TLE, which is required for repression. Although the Qdomain is required for oligomerization, its structural properties have never been fully characterized. Here, the Qdomain was tagged with a small ubiquitinrelated modifier protein (SUMO) to alleviate aggregation observed with the untagged Qdomain. Size exclusion chromatography (Gel Filtration) and analytical ultracentrifugations were performed. Results show that SUMOQ oligomerizes predominantly as a tetramer. However, significant heterogeneity is observed at high salt concentrations. Analysis of the hydrodynamic data suggest a markedly nonspherical structure.
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