ISSN:
1573-4978
Keywords:
Nuclear Factor I
;
proline-rich domain
;
transcription activator
;
yeast
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A full-length cDNA of the rat liver Nuclear Factor 1 (NF1L21) has been cloned and expressed inS. 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00997237
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