Acidic activation domain

SwAFEiELD, J. C., Bromber, J. F., and Johnston, S. A. Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4. Nature 1992, 357, 698-700. 

Tumbar, T., Sudlow, G., and Belmont, A.S. (1999) Large-scale chromatin unfolding and remodeling induced by VP16 acidic activation domain. J. Cell Biol. 145, 1341-1354. 

A Etchegaray, R Dieckmann, J Kennedy, G Turner, H von Dohren. ACV synthetase expression of amino acid activating domains of the Penicillium chrysogenum enzyme in Aspergillus nidulans. Biochem Biophys Res Commun 237 166-169, 1997. 

A Doller, A Haese, R Zocher. Molecular cloning of the amino acid activation domain of enniatin synthetase from Fusarium sambucinum. Symposium Enzymology of Biosynthesis of Natural Products, Abstract 66, Technische Universitat Berlin, September 22-25, 1996. 

May JJ, Kessler N, Marahiel MA, Stubbs MT. Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. U.S.A. 2002 99 12120-12125. 

Thus the acidic activation domain in CREB and the ligandbinding activation domains in nuclear receptors represent... 

VPl could bind to the ABRE-ABF complex either through protein-DNA or protein-protein contacts and activate transcription by means of the acidic activator domain. 

ACID-ACTIVATING DOMAIN AND IDENTIFICATION OF ADENYLATINC AND THIOLESTER MODULES... 

Fifure 4 The rype 1 amino acid-activating domain. A schematic diagram of the peptide yri thecase amino acid-activating domain I showing the locations of the adenylation and thioester modules along with the sites of the six conserved core sequences. The consensus amino acid sequence of each core sequence is shown. Amino acid positions labeled are the sites of amino acid substitutions that reduce adenylation activity. The position labeled t is the sice of one of the substitutions in a double mutant with reduced adenylating activity. The amino acid position labeled indicates the site of an amino acid substitution that eliminates thioester activity. 

Figure 6 The type II, or N-methyl-amino acid-activating, domain. As in Figure 4, the amino acid-activating domain is shown with aJenylating and thioester modules, the ATP-binding region, and the six conserved core sequences. The SAM-dependent N-methyltransferase module i also shown.

D Souza C, Nakano MM, Corbell N, Zuber P. Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase Effects on sutfactin production and competence development in Bacillus subtilis. J Bacterial 1993 175 3502-3510. 

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