The Bcl10 gene has recently been cloned from the chromosomal translocation t(1:14) (p22; q32) in a low-grade mucosa-associated lymphoid tissue (MALT) lymphoma, and was implicated in the pathogenesis of this and several other tumor types. In yeast two hybrid systems, when it was fused to Gal4 DNA-binding domain of pGBT9, this fusion protein can activate the expression of reporter genes without Gal4-AD domain. Through deletion assay and secondary structure prediction, we found that the N-terminal of Bcl10 contributed more to activation than the C-terminal. It has been recently reported that Bcl10 expression is correlated with the activation of NF-kappaB in eukaryotic cells, so it may represent an important role in protein expression. Our research is the first to demonstrate a new function of Bcl10: transcription activation in yeast.