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Science 11 February 1994: Vol. 263. no. 5148, pp. 808 - 811 DOI: 10.1126/science.8303297
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Articles
Science, Vol 263, Issue 5148, 808-811
Copyright © 1994 by American Association for the Advancement of Science
Transcriptional activation modulated by homopolymeric glutamine and proline stretches
HP Gerber,
K Seipel,
O Georgiev,
M Hofferer,
M Hug,
S Rusconi,
and
W Schaffner
Institut fur Molekularbiologie II der Universitat Zurich, Switzerland.
Many transcription factors contain proline- or glutamine-rich activation domains. Here it is shown that simple homopolymeric stretches of these amino acids can activate transcription when fused to the DNA binding domain of GAL4 factor. In vitro, activity increased with polymer length, whereas in cell transfection assays maximal activity was achieved by 10 to 30 glutamines or about 10 prolines. Similar results were obtained when glutamine stretches were placed within a [GAL4]-VP16 chimeric protein. Because these stretches are encoded by rapidly evolving triplet repeats (microsatellites), they may be the main cause for modulation of transcription factor activity and thus result in subtle or overt genomic effects.
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- Histone deacetylase inhibitors reduce polyglutamine toxicity.
- A. McCampbell, A. A. Taye, L. Whitty, E. Penney, J. S. Steffan, and K. H. Fischbeck (2001)
PNAS
98, 15179-15184
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