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Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4

Nature volume 357, pages 698–700 (1992)Cite this article

An Erratum to this article was published on 31 December 1992

Abstract

THE acidic transcriptional activation motif functions in all eukary-otes1–4, which suggests that it makes contact with some universal component of the transcriptional apparatus. Transcriptional activation by the yeast regulatory protein GAL4 requires an acidic region at its carboxyl terminus. Here we implement a selection scheme to determine whether GAL4 can still function when this C-terminal domain has been deleted. It can, when accompanied by a mutation in the SUG1gene which is an essential gene in yeast. Analysis of mutant SUG1in combination with various alleles of GAL4 indicates that SUG1 acts through a transcriptional pathway that depends on GAL4, but requires a region of GAL4 other than the C-terminal acidic activation domain. The predicted amino-acid sequence of SUG1 closely resembles that of two human proteins, TBP1 and MSS1, which modulate expression mediated by the human immunodeficiency virus tatgene.

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Author notes

  1. Jacqueline F. Bromberg

    Present address: Department of Internal Medicine, Barnes Hospital, St Louis, Missouri, 63110, USA

  2. Stephen A Johnston: To whom correspondence should be addressed

Affiliations

  1. Department of Medicine, University of Texas Southwestern Medical Center, 5323 Harry Mines Boulevard, Dallas, Texas, 75235-8573, USA

    Jonathan C. Swaffield, Jacqueline F. Bromberg & Stephen A. Johnston

  2. Departments of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Mines Boulevard, Dallas, Texas, 75235-8573, USA

    Stephen A. Johnston

Authors
  1. Jonathan C. Swaffield
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  2. Jacqueline F. Bromberg
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  3. Stephen A. Johnston
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Swaffield, J., Bromberg, J. & Johnston, S. Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4. Nature 357, 698–700 (1992). https://doi.org/10.1038/357698a0

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