The UGA43 gene of Saccharomyces cerevisiae is required for repression of inducible genes involved in the utilization of 4-aminobutyric acid (GABA) or urea as nitrogen sources. The UGA43 gene has been cloned by complementation of a uga43 mutation. The N-terminal region of the UGA43 protein is very similar to the DNA-binding zinc-finger region typical of the GATA regulatory factor family in vertebrates. UGA43 is the first reported instance of a GATA protein with a negative regulatory function. The C-terminal region of the predicted UGA43 protein contains a putative leucine zipper. Sequencing of three uga43 mutant alleles suggests that the GATA and putative leucine-zipper regions are both required for the repressive activity of UGA43. UGA43 appears to be a highly regulated gene. On "poor" nitrogen sources, UGA43 transcripts are measured at high levels whereas they are nearly undetectable in conditions of nitrogen catabolite repression. The levels measured on "poor" nitrogen sources are further increased in uga43 mutant cells, suggesting that UGA43 exerts negative autoregulation.
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http://dx.doi.org/10.1007/BF00351687 | DOI Listing |
Int J Biochem Cell Biol
December 2001
Centro de Investigaciones sobre Porfirinas y Porfirias. CIPYP (CONICET, FCEyN, UBA), Ciudad Universitaria, Pabellón II, 2nd Piso, (1428), Buenos Aires, Argentina.
Background And Aims: biological processes in all organisms are controlled by environmental conditions, however, information concerning the molecular responses to external pH is scarce. In this work we studied the pH response of UGA4 gene encoding delta-aminolevulinic acid and gamma-aminobutyric acid permease in Saccharomyces cerevisiae.
Methods: we analyzed the effect of pH on the expression of UGA4 gene measuring beta-galactosidase activity in cells carrying a UGA4::lacZ fusion gene.
J Bacteriol
July 1998
Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico.
Saccharomyces cerevisiae glutamate synthase (GOGAT) is an oligomeric enzyme composed of three 199-kDa identical subunits encoded by GLT1. In this work, we analyzed GLT1 transcriptional regulation. GLT1-lacZ fusions were prepared and GLT1 expression was determined in a GDH1 wild-type strain and in a gdh1 mutant derivative grown in the presence of various nitrogen sources.
View Article and Find Full Text PDFMol Microbiol
March 1997
Laboratoire de Physiologie Cellulaire et de Génétique des Levures, Université Libre de Bruxelles, Belgium.
In Saccharomyces cerevisiae, two positive transcription factors of the GATA family, Gln3p and Nil1p/Gat1p, upregulate the expression of multiple nitrogen pathway genes via upstream 5'-GATA-3' sequences. Another GATA factor, Uga43p/Dal80p, downregulates to varying degrees the expression of some nitrogen-regulated genes. Here, we report the functional analysis of a fourth GATA factor, Gzf3p/Nil2p, whose gene was discovered by systematic sequencing of chromosome X.
View Article and Find Full Text PDFNucleic Acids Res
February 1995
Laboratoire de Physiologie Cellulaire et de Génétique des Levures, Université Libre de Bruxelles, Belgium.
The S. cerevisiae Uga43(Dal80) protein down-regulates the expression of multiple nitrogen pathway genes. It contains a zinc-finger motif similar to the DNA-binding domain of the vertebrate GATA family of transcription factors; this domain is known to direct binding to 5'-GATA-3' core sequences.
View Article and Find Full Text PDFMol Gen Genet
February 1993
Laboratoire de Physiologie Cellulaire et de Génétique des Levures, Université Libre de Bruxelles, Belgium.
Transport of 4-aminobutyric acid (GABA) in Saccharomyces cerevisiae is mediated by three transport systems: the general amino acid permease (GAP1 gene), the proline permease (PUT4 gene), and a specific GABA permease (UGA4 gene) which is induced in the presence of GABA. The UGA4 gene encoding the inducible GABA-specific transporter was cloned and sequenced and its expression analyzed. The predicted amino acid sequence shows that UGA4 encodes a 62 kDa protein having 9-12 putative membrane-spanning regions.
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