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Science 4 January 1991: Vol. 251. no. 4989, pp. 87 - 90 DOI: 10.1126/science.1846049
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Articles
Science, Vol 251, Issue 4989, 87-90
Copyright © 1991 by American Association for the Advancement of Science
Critical structural elements of the VP16 transcriptional activation domain
WD Cress
and
SJ Triezenberg
Department of Biochemistry, Michigan State University, East Lansing 48824-1319.
Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component of the activation domain. A phenylalanine residue at position 442 was exquisitely sensitive to mutation. Transcriptional activators of several classes contain hydrophobic amino acids arranged in patterns resembling that of VP16. Therefore, the mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules.
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- X. Yang, K. Su, M. D. Roos, Q. Chang, A. J. Paterson, and J. E. Kudlow (2001)
PNAS
98, 6611-6616
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- N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the Host Cell Factor-1 binding motif.
- R. L. Luciano and A. C. Wilson (2000)
PNAS
97, 10757-10762
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