Abstract
A full-length cDNA of the rat liver Nuclear Factor 1 (NF1L21) has been cloned and expressed in S. cerevisiae to analyse the architecture of its activation domain. NF1L21 displays a specific DNA-binding activity, as well as the ability to activate transcription from an artificial NF1-responsive promoter in yeast. Interaction of two or more NF1L21 molecules with multiple sites on the same promoter activated transcription in a synergistic fashion. Functional analysis of the activation domain of NF1L21 reveals a tripartite structure. Two distinct positive elements are required for NF1L21-mediated transcription activation. A proline-rich element sandwiched between these two positive domains attenuates their transactivation potential. A shorter NF1L variant (NF1L4) in which the distal positive element is replaced by a different sequence was also isolated. NF1L4 displays the same DNA-binding activity and dimerisation properties as NF1L21, but is unable to activate transcription in yeast.
Original language | English |
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Pages (from-to) | 147-158 |
Number of pages | 12 |
Journal | Molecular biology reports |
Volume | 21 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1 Oct 1995 |
Keywords / Materials (for Non-textual outputs)
- nuclear factor I
- proline-rich domain
- transcription activator
- yeast