Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein.

Abstract:

:Derivatives of the yeast GCN4 transcription factor containing acidic regions of 35 to 40 amino acids fused directly to the DNA-binding domain are fully functional in vivo. High resolution deletion analysis and proteolytic mapping suggest that the activation region is a repeated structure composed of small units acting additively. Acidic character is a feature of the structural motif, possibly a dimer of alpha-helices from two GCN4 monomers, that may be important for interactions with the basic transcriptional machinery.

journal_name

Nature

journal_title

Nature

authors

Hope IA,Mahadevan S,Struhl K

doi

10.1038/333635a0

subject

Has Abstract

pub_date

1988-06-16 00:00:00

pages

635-40

issue

6174

eissn

0028-0836

issn

1476-4687

journal_volume

333

pub_type

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