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J Biol Chem, Vol. 275, Issue 10, 7198-7204, March 10, 2000

Functional Domain Mapping and Subcellular Distribution of Dal82p in Saccharomyces cerevisiae*

Stephanie Scott, Rosemary DorringtonDagger , Vladimir Svetlov§, Alexander E. Beeser, Mackenzie Distler, and Terrance G. Cooper

From the Department of Microbiology and Immunology, University of Tennessee, Memphis, Tennessee 38163

Previous studies have shown that (i) Dal81p and Dal82p are required for allophanate-induced gene expression in Saccharomyces cerevisiae; (ii) the cis-acting element mediating the induced transcriptional response to allophanate is a dodecanucleotide, UISALL; and (iii) Dal82p binds specifically to UISALL. Here we show that Dal82p is localized to the nucleus and parallels movement of the DNA through the cell cycle. Deletion analysis of DAL82 identified and localized three functional domains. Electrophoretic mobility shift assays identified a peptide (consisting of Dal82p amino acids 1-85) that is sufficient to bind a DNA fragment containing UISALL. LexA-tethering experiments demonstrated that Dal82p is capable of mediating transcriptional activation. The activation domain consists of two parts: (i) an absolutely required core region (amino acids 66-99) and (ii) less well defined regions flanking residues 66-99 that are required for full wild-type levels of activation. The Dal82p C terminus contains a predicted coiled-coil motif that down-regulates Dal82p-mediated transcriptional activation.

* The work was supported by United States Public Health Service Grant GM-35642.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Biochemistry and Microbiology, Rhodes University, P. O. Box 94, Grahamstown 6140, South Africa.

§ Present address: Dept. of Oncology, McArdle Laboratory for Cancer Research, University of Wisconsin, Madison, WI 53706.

To whom correspondence should be addressed. Tel.: 901-448-6175; Fax: 901-448-8462; E-mail: tcooper@utmem1.utmem.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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