The GLN3 gene product is required for transcriptional activation of allantoin system gene expression in Saccharomyces cerevisiae

Cooper, Terrance G.; Ferguson, David O.; Rai, Rajendra; Bysani, Nanda

doi:10.1128/jb.172.2.1014-1018.1990

Cited by 83 publications

(61 citation statements)

References 23 publications

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“…For example, they may be incapable of absorbing USA due to a mutation of the DAL5 transporter gene (Turoscy and Cooper, 1987) or of GLN3, which encodes a transcription factor required for DAL5 transcription (Cooper et al, 1990;Mitchell and Magasanik, 1984). Alternatively, the cells may be able to absorb USA but be unable to convert it into uracil due to mutation of a gene required for uracil biosynthesis downstream of the USA step, such as the URA3 gene.…”

Section: Mutants Defective For the Propagation Of [Ure3]mentioning

confidence: 99%

[URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast

Roberts

Moriyama

Wickner

2003

Yeast

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Section: Mutants Defective For the Propagation Of [Ure3]mentioning

confidence: 99%

[URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast

Roberts

Moriyama

Wickner

2003

Yeast

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“…For instance, in cells grown under conditions of nitrogen derepression, high-level expression of the allantoate permease gene DAL5 is largely dependent on Gln3p (Cooper et a/., 1990). Gln3p-activated expression is sensitive to nitrogen repression (Mitchell and Magasanik, 1984;Magasanik, 1992).…”

Section: Introductionmentioning

confidence: 99%

Gzf3p, a fourth GATA factor involved in nitrogen‐regulated transcription in Saccharomyces cerevisiae

Soussi‐Boudekou

Vissers

Urrestarazu

et al. 1997

Molecular Microbiology

101

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Summary In Saccharomyces cerevisiae, two positive transcription factors of the GATA family, Gln3p and NiMp/ Gatlp, upregulate the expression of multiple nitrogen pathway genes via upstream 5‐GATA‐3′ sequences. Another GATA factor, Uga43p/Da180p, downregulates to varying degrees the expression of some nitrogen‐regulated genes. Here, we report the functional analysis of a fourth GATA factor, Gzf 3p/Ni12p, whose gene was discovered by systematic sequencing of chromosome X. The Gzf3 protein most closely resembles Uga43p. Similar to Uga43p, Gzf3p has the properties of a negative GATA factor. While Uga43p is active specifically under nitrogen‐derepression conditions, Gzf 3p exerts its negative regulatory function specifically on preferred nitrogen sources: it is involved in nitrogen repression of NiMp‐dependent transcription. At least one positive GATA factor is required for the UGA43 and GZF3 genes to be expressed. The Uga43p factor negatively regulates GZF3 expression and vice versa. In addition, both Uga43p and Gzf3p moderately regulate expression of their own genes. These two proteins seem to be parts of a complex network of GATA factors which probably play a determining role in nitrogen‐regulated transcription.

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“…Parallel evidence showed that the nonchromosomal gene [PSI] is a prion form of Sup35p (10). Ure2p is a regulator of nitrogen catabolism that acts in the cytoplasm by complexing with the GATA transcription factor Gln3p, preventing entry of the latter into the nucleus (12)(13)(14)(15)(16)(17)(18). Ure2p suffices to carry out the prion domain functions (19,20), but Ure2p 1-80 is even more efficient (21).…”

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confidence: 99%

Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein

Baxa

Speransky

Steven

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

157

149

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The [URE3] infectious protein (prion) of Saccharomyces cerevisiae is a self-propagating amyloid form of Ure2p. The C-terminal domain of Ure2p controls nitrogen catabolism by complexing with the transcription factor, Gln3p, whereas the asparagine-rich Nterminal ''prion'' domain is responsible for amyloid filament formation (prion conversion). On filament formation, Ure2p is inactivated, reflecting either a structural change in the C-terminal domain or steric blocking of its interaction with Gln3p. We fused the prion domain with four proteins whose activities should not be sterically impeded by aggregation because their substrates are very small: barnase, carbonic anhydrase, glutathione S-transferase, and green fluorescent protein. All formed amyloid filaments in vitro, whose diameters increased with the mass of the appended enzyme. The helical repeat lengths were consistent within a single filament but varied with the construct and between filaments from a single construct. CD data suggest that, in the soluble fusion proteins, the prion domain has no regular secondary structure, whereas earlier data showed that in filaments, it is virtually all ␤-sheet. In filaments, the activity of the appended proteins was at most mildly reduced, when substrate diffusion effects were taken into account, indicating that they retained their native structures. These observations suggest that the amyloid content of these filaments is confined to their prion domain-containing backbones and imply that Ure2p is inactivated in [URE3] cells by a steric blocking mechanism.

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The GLN3 gene product is required for transcriptional activation of allantoin system gene expression in Saccharomyces cerevisiae

Cited by 83 publications

References 23 publications

[URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast

[URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast

Gzf3p, a fourth GATA factor involved in nitrogen‐regulated transcription in Saccharomyces cerevisiae

Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein

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