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J. Biol. Chem., Vol. 275, Issue 23, 17611-17618, June 9, 2000
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From the Department of Microbiology and Immunology, University of
Tennessee, Memphis, Tennessee 38163
Saccharomyces cerevisiae selectively
uses good nitrogen sources (glutamine) in preference to poor ones
(proline) by repressing GATA factor-dependent transcription
of the genes needed to transport and catabolize poor nitrogen sources,
a physiological process designated nitrogen catabolite repression
(NCR). We show that some NCR-sensitive genes (CAN1,
DAL5, DUR1,2, and DUR3) produce two
transcripts of slightly different sizes. Synthesis of the shorter
transcript is NCR-sensitive and that of the longer transcript is not.
The longer transcript also predominates in gln3
Saccharomyces cerevisiae GATA Sequences Function as
TATA Elements during Nitrogen Catabolite Repression and When Gln3p Is
Excluded from the Nucleus by Overproduction of Ure2p*
,
mutants irrespective of the nitrogen source provided. We demonstrate that the
longer mRNA species arises through the use of an alternative transcription start site generated by Gln3p-binding sites (GATAAs) being able to act as surrogate TATA elements. The ability of GATAAs to
serve as surrogate TATAs, i.e. when synthesis of the
shorter, NCR-sensitive transcripts are inhibited, correlates with
sequestration of enhanced green fluorescent protein (EGFP)-Gln3p in the
cytoplasm in a way that is indistinguishable from that seen with
EGFP-Ure2p. However, when the shorter, NCR-sensitive DAL5
transcript predominates, EGFP-Gln3p is nuclear. These data suggest that
the mechanism underlying NCR involves the cytoplasmic association of
Ure2p with Gln3p, an interaction that prevents Gln3p from reaching it
is binding sites upstream of NCR-sensitive genes.
*
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.
Present address: Division of Vaccines and Related Products
Applications, OVRR/CBER, Food and Drug Administration, Woodmont Office
Center I, HFM-475 Suite 370 North, 1401 Rockville Pike, Rockville, MD
20852-1448.
§
Present address: College of Medical Sciences, Nova Southeastern
University, 3200 South University Dr., Fort Lauderdale, FL 33328-2018.
¶
To whom correspondence should be addressed. Tel.:
901-448-6175; Fax: 901-448-8462; E-mail: tcooper@utmem.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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