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Nanog is a newly identified divergent homeodo-main protein that directs the infinite propagation and sustains the pluripotency of embryonic stem cels. It has been reported that murine Nanog has two potent transactivation domains in N-terminal and C-terminal regions. Human Nanog (hNanog) to the open reading frame and homeodomain of murine Nanog, respectively. However, the func-tional domains and molecular mechanisms of hNanog are poorly understood. In this study, for the first time, we presented that only C-terminus of hNanog contains a potent transactivation do-main. Based on the amino acid sequences of homeobox domain, we roughly divided hNanog open reading frame into the thre regions such as N-terminal, homeodomain and C-terminal re-gions and constructed either the fusion pro-binding domain or the context of native hNanog protein. Reporter asays by using reporter pla-mid containing Gal4 or Nanog binding site revealed that the only C-terminal region exhibited the significant fold induction of transactivation. However, interestingly, there was no significant activation through N-terminal region unlike mu-rine Nanog, suggesting that C-terminal region may have more critical roles in the transcriptional activation of target genes. Taken together, the finding of a putative transactivation domain in hNanog may contribute to the further understand-downstream genes involved in self-renewal and pluripotency of human stem cels.

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