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J. Biol. Chem., Vol. 276, Issue 34, 32136-32144, August 24, 2001
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From the Department of Molecular Sciences, University of Tennessee,
Memphis, Tennessee 38163
Gln3p is one of two well characterized GATA
family transcriptional activation factors whose function is regulated
by the nitrogen supply of the cell. When nitrogen is limiting, Gln3p
and Gat1p are concentrated in the nucleus where they bind GATA
sequences upstream of nitrogen catabolite repression (NCR)-sensitive
genes and activate their transcription. Conversely, in excess nitrogen, these GATA sequences are unoccupied by Gln3p and Gat1p because these
transcription activators are excluded from the nucleus. Ure2p binds to
Gln3p and Gat1p and is required for NCR-sensitive transcription to be
repressed and for nuclear exclusion of these transcription factors.
Here we show the following. (i) Gln3p residues 344-365 are required
for nuclear localization. (ii) Replacing Ser-344, Ser-347, and Ser-355
with alanines has minimal effects on GFP-Gln3p localization. However,
replacing Gln3p Ser-344, Ser-347, and Ser-355 with aspartates results
in significant loss of its ability to be concentrated in the nucleus.
(iii) N and C termini of the Gln3p region required for it to complex
with Ure2p and be excluded from the nucleus are between residues 1-103
and 301-365, respectively. (iv) N and C termini of the Ure2p region
required for it to interact with Gln3p are situated between residues
101-151 and 330-346, respectively. (v) Loss of Ure2p residues
participating in either dimer or prion formation diminishes its ability
to carry out NCR-sensitive regulation of Gln3p activity.
Gln3p Nuclear Localization and Interaction with Ure2p in
Saccharomyces cerevisiae*
*
This work was supported by National Institutes of Health
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.
To whom correspondence should be addressed. Tel.: 901-448-6179;
Fax: 901-448-8462; E-mail: tcooper@utmem.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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