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J. Biol. Chem., Vol. 277, Issue 40, 37559-37566, October 4, 2002
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From the Department of Molecular Sciences, University of Tennessee,
Memphis, Tennessee 38163
Regulated intracellular localization of Gln3, the
transcriptional activator responsible for nitrogen catabolite
repression (NCR)-sensitive transcription, permits Saccharomyces
cerevisiae to utilize good nitrogen sources (e.g.
glutamine and ammonia) in preference to poor ones
(e.g. proline). During nitrogen starvation or growth in
medium containing a poor nitrogen source, Gln3 is nuclear and
NCR-sensitive transcription is high. However, when cells are grown in
excess nitrogen, Gln3 is localized to the cytoplasm with a concomitant
decrease in gene expression. Treating cells with the Tor protein
inhibitor, rapamycin, mimics nitrogen starvation. Recently, carbon
starvation has been reported to cause nuclear localization of Gln3 and
increased NCR-sensitive transcription. Here we show that nuclear
localization of Gln3 during carbon starvation derives from its indirect
effects on nitrogen metabolism, i.e. Gln3 does not move
into the nucleus of carbon-starved cells if glutamine rather than
ammonia is provided as the nitrogen source. In addition, these studies
have clearly shown Gln3 is not uniformly distributed in the cytoplasm,
but rather localizes to punctate or tubular structures. Analysis of
these images by deconvolution microscopy suggests that Gln3 is
concentrated in or associated with a highly structured system in the
cytosol, one that is possibly vesicular in nature. This finding may
impact significantly on how we view (i) the mechanism by which Tor
regulates the intracellular localization of Gln3 and (ii) how proteins
move into and out of the nucleus.
Cytoplasmic Compartmentation of Gln3 during Nitrogen Catabolite
Repression and the Mechanism of Its Nuclear Localization during Carbon
Starvation 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: 901-448-3244; E-mail: tcooper@utmem.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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