Advanced search×

A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor.

Cell 43(3 Pt 2):729-36 (1985) PMID 3907859

We describe a new protein that binds to DNA and activates gene transcription in yeast. This protein, LexA-GAL4, is a hybrid of LexA, an Escherichia coli repressor protein, and GAL4, a Saccharomyces cerevisiae transcriptional activator. The hybrid protein, synthesized in yeast, activates transcription of a gene if and only if a lexA operator is present near the transcription start site. Thus, the DNA binding function of GAL4 can be replaced with that of a prokaryotic repressor without loss of the transcriptional activation function. These results suggest that DNA-bound LexA-GAL4 and DNA-bound GAL4 activate transcription by contacting other proteins.

DOI: 10.1016/0092-8674(85)90246-6
Version: za2963e q8za2 q8zb7 q8zc4 q8zd5 q8zec q8zf8 q8zg3

Similar articles you may find interesting…

  1. Transcription Dynamics

    Mol Cell 35(6):741-753 (2009) PMID 19782025

    All aspects of transcription and its regulation involve dynamic events. The basal transcription machinery and regulatory components are dynamically recruited to their target genes, and dynamic interactions of transcription factors with chromatin--and with each other--play a key role in RNA polymeras...
  2. Building an artificial regulatory system to understand a natural one

    Cell (2004) PMID 15055588

  3. Five intermediate complexes in transcription initiation by RNA polymerase II.

    Cell 56(4):549-61 (1989) PMID 2917366

    I footprint analysis. TFIIA, derived from yeast or mammalian cells, formed a complex with yeast TFIID and the TATA element. TFIIB bound to this complex and probably acts as a "bridge" to the polymerase and the initiation site. The addition of ATP or dATP, necessary for "activation" of transcription,...