Extensive mutagenesis of a transcriptional activation domain identifies single hydrophobic and acidic amino acids important for activation in vivo.

Molecular and Cellular Biology
M B SainzV L Chandler

Abstract

C1 is a transcriptional activator of genes encoding biosynthetic enzymes of the maize anthocyanin pigment pathway. C1 has an amino terminus homologous to Myb DNA-binding domains and an acidic carboxyl terminus that is a transcriptional activation domain in maize and yeast cells. To identify amino acids critical for transcriptional activation, an extensive random mutagenesis of the C1 carboxyl terminus was done. The C1 activation domain is remarkably tolerant of amino acid substitutions, as changes at 34 residues had little or no effect on transcriptional activity. These changes include introduction of helix-incompatible amino acids throughout the C1 activation domain and alteration of most single acidic amino acids, suggesting that a previously postulated amphipathic alpha-helix is not required for activation. Substitutions at two positions revealed amino acids important for transcriptional activation. Replacement of leucine 253 with a proline or glutamine resulted in approximately 10% of wild-type transcriptional activation. Leucine 253 is in a region of C1 in which several hydrophobic residues align with residues important for transcriptional activation by the herpes simplex virus VP16 protein. However, changes at all other h...Continue Reading

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Citations

Oct 21, 2014·The New Phytologist·Nick W AlbertWarren M Williams
Jul 11, 2012·Proceedings of the National Academy of Sciences of the United States of America·Que KongLing Yuan
Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·C. SchwechheimerM. W. Bevan
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Jan 26, 2020·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·Toshiyuki KomoriToshihiko Komari

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