ArticleThe Journal of biological chemistry2000
Roles of the Dal82p domains in allophanate/oxalurate-dependent gene expression in Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
- A novel aminotransferase gene and its regulator acquired in Saccharomyces by a horizontal gene transfer event.BMC biology · 2023Article
- Temporal expression profiling identifies pathways mediating effect of causal variant on phenotype.PLoS genetics · 2015Article
- gln3 mutations dissociate responses to nitrogen limitation (nitrogen catabolite repression) and rapamycin inhibition of TorC1.The Journal of biological chemistry · 2013Article
- Review
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- Recent advances in nitrogen regulation: a comparison between Saccharomyces cerevisiae and filamentous fungi.Eukaryotic cell · 2008Review
- An improved map of conserved regulatory sites for Saccharomyces cerevisiae.BMC bioinformatics · 2006Article
- Antithetic effects of MBD2a on gene regulation.Molecular and cellular biology · 2003Article
- Gln3p nuclear localization and interaction with Ure2p in Saccharomyces cerevisiae.The Journal of biological chemistry · 2001Article
- Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Allophanate/oxalurate-induced gene expression in Saccharomyces cerevisiae requires at least five transcription factors, four of which act positively (Gln3p, Gat1p, Dal81p, and Dal82p) and one negatively (Dal80p). Gln3p binds to and Gat1p is proposed to bind to single GATA sequences; Dal80p binds to pairs of specifically oriented and spaced GATA sequences, and Dal82p binds to a pathway-specific element, UIS(ALL). Dal82p consists of at least three domains as follows: (i) UIS(ALL) DNA-binding, (ii) transcriptional activation, and (iii) coiled-coil(DAL82). Here we show that the coiled-coil(DAL82) domain possesses two demonstrable functions. (i) It prevents Dal82p-mediated transcription when inducer is absent. (ii) It is a major, although not exclusive, domain through which the inducer signal is received. Supporting the latter conclusion, a 38-amino acid fragment, containing little more than the coiled-coil(DAL82) domain, supports oxalurate-inducible, Dal81p-dependent, reporter gene transcription. Dal81p is required for inducer responsiveness of LexAp-Dal82p and LexAp coiled-coil(DAL82)-mediated transcription but isn't needed for inducer-dependent activation mediated by a Dal82p containing deletions in both the coiled-coil(DAL82), UIS(ALL)-binding domains. There may be an interaction between Dal81p and the coiled-coil(DAL82) domain since (i) Dal81p is required for transcription mediated by LexA-coiled-coil(DAL82)p and (ii) a Dal81p-Dal82p complex is detected by two-hybrid assay.
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