GAL4-lϰBα and GAL4-lϰBγ activate transcription by different mechanisms (original) (raw)
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Department of Biology, Boston University
5 Cummington Street, Boston, MA 02215, USA
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Department of Biology, Boston University
5 Cummington Street, Boston, MA 02215, USA
Search for other works by this author on:
Department of Biology, Boston University
5 Cummington Street, Boston, MA 02215, USA
*To whom correspondence should be addressed
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Received:
28 December 1992
Revision received:
19 March 1993
Cite
Patrice J. Morin, Gita S. Subramanian, Thomas D. Gilmore, GAL4-lϰBα and GAL4-lϰBγ activate transcription by different mechanisms, Nucleic Acids Research, Volume 21, Issue 9, 11 May 1993, Pages 2157–2163, https://doi.org/10.1093/nar/21.9.2157
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Abstract
IϰB proteins regulate Rel/NF-ϰB transcription complexes through a direct protein-protein Interaction. In addition, we have previously shown that certain IϰB proteins (IϰBα and IϰBγ) can act as activators of transcription when fused to the DNA-binding domain of GAL4. We now show that a mutant chicken IϰBα protein that cannot Interact with Rel proteins In vitro did not activate transcription when fused to GAL4 In chicken embryo flbroblasts (CEF) and Saccharomyces cerevlslae, and did not Inhibit growth In yeast; in contrast, an IϰBα mutant that can still interact In vitro with Rel proteins activated transcription In both CEF and yeast and inhibited growth in yeast. In CEF, GAL4-IϰBα mediated transcription activation was Inhibited by co-transfectlon with an expression vector for a RelA (p65) protein that contained sequences needed for interaction with IϰBα but that was deleted of its transcription activation domain. Therefore, it appears that GAL4-IϰBα activates transcription by interacting with an endogenous Rel family protein in CEF. In contrast, the activation domain from IϰBγ behaved as a genuine acidic activator of transcription and did not inhibit growth when expressed in yeast. Since transcription activation and growth Inhibition by GAL4-lIϰBαmutants In yeast correlated with their ability to interact with vertebrate Rel proteins, our results suggest that these activities of GAL4-lIϰBα are mediated through Interaction with a Rel-like protein In yeast, which Is Important for cell growth.
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