Cloning and Characterization of a General Amino Acid Control Transcriptional Activator from the Chestnut Blight FungusCryphonectria parasitica

Wang, Ping; Larson, Thomas; Chen, Chein-Hwa; Pawlyk, Diane M.; Clark, Julie; Nuss, Donald L.

doi:10.1006/fgbi.1997.1023

Cited by 28 publications

(15 citation statements)

References 69 publications

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“…G proteins are not the only regulatory mechanisms governing virulence in C. parasitica. Regulatory pathways, including the IP 3 -Ca 2ϩ -calmodulin-calcineurin pathway and the general amino acid control pathway that is activated in response to amino acid starvation, are also important in regulating pigment production and virulence (152,291). Infection of C. parasitica by the virus HAV1 causes a broad range of phenotypic changes, many of which mimic phenotypes of mutant strains with defects in G protein signaling.…”

Section: Virulence Attenuationmentioning

confidence: 99%

Signal Transduction Cascades Regulating Fungal Development and Virulence

Lengeler

Davidson

D’Souza

et al. 2000

Microbiol Mol Biol Rev

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831

774

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SUMMARY Cellular differentiation, mating, and filamentous growth are regulated in many fungi by environmental and nutritional signals. For example, in response to nitrogen limitation, diploid cells of the yeast Saccharomyces cerevisiae undergo a dimorphic transition to filamentous growth referred to as pseudohyphal differentiation. Yeast filamentous growth is regulated, in part, by two conserved signal transduction cascades: a mitogen-activated protein kinase cascade and a G-protein regulated cyclic AMP signaling pathway. Related signaling cascades play an analogous role in regulating mating and virulence in the plant fungal pathogen Ustilago maydis and the human fungal pathogens Cryptococcus neoformans and Candida albicans. We review here studies on the signaling cascades that regulate development of these and other fungi. This analysis illustrates both how the model yeast S. cerevisiae can serve as a paradigm for signaling in other organisms and also how studies in other fungi provide insights into conserved signaling pathways that operate in many divergent organisms.

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Section: Virulence Attenuationmentioning

confidence: 99%

Signal Transduction Cascades Regulating Fungal Development and Virulence

Lengeler

Davidson

D’Souza

et al. 2000

Microbiol Mol Biol Rev

Self Cite

831

774

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“…These sequences of the C-terminal half characterize Gcn4p as a member of the bZIP-type transcriptional activator family. Homologs of GCN4, whose products contain the typical bZIP-type structures, were isolated in A. niger (cpcA; Wanke et al, 1997), N. crassa (cpc-1; Paluh et al, 1988;Paluh and Yanofsky, 1991), and Cryphonectria parasitica (cpCPC1; Wang et al, 1998). Detailed functional analyses of domains of fungal bZIP proteins have previously been performed for Gcn4p (Kornitzer et al, 1994;Drysdale et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional Autoregulation and Inhibition of mRNA Translation of Amino Acid Regulator GenecpcAof Filamentous FungusAspergillus nidulans

Hoffmann

Valerius

Andermann

et al. 2001

MBoC

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The CPCA protein of the filamentous fungus Aspergillus nidulans is a member of the c-Jun-like transcriptional activator family. It acts as central transcription factor of the cross-pathway regulatory network of amino acid biosynthesis and is functionally exchangeable for the general control transcriptional activator Gcn4p of Saccharomyces cerevisiae. In contrast to GCN4, expression of cpcA is strongly regulated by two equally important mechanisms with additive effects that lead to a fivefold increased CPCA protein amount under amino acid starvation conditions. One component of cpcA regulation involves a transcriptional autoregulatory mechanism via a CPCA recognition element (CPRE) in the cpcA promoter that causes a sevenfold increased cpcA mRNA level when cells are starved for amino acids. Point mutations in the CPRE cause a constitutively low mRNA level of cpcA and a halved protein level when amino acids are limited. Moreover, two upstream open reading frames (uORFs) in the 5Ј region of the cpcA mRNA are important for a translational regulatory mechanism. Destruction of both short uORFs results in a sixfold increased CPCA protein level under nonstarvation conditions and a 10-fold increase under starvation conditions. Mutations in both the CPRE and uORF regulatory elements lead to an intermediate effect, with a low cpcA mRNA level but a threefold increased CPCA protein level independent of amino acid availability. These data argue for a combined regulation of cpcA that includes a translational regulation like that of yeast GCN4 as well as a transcriptional regulation like that of the mammalian jun and fos genes.

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“…The ultimate element of the signal transduction pathway, a transcriptional activator protein, is encoded by the homologous genes, cpc-1 of N. crassa (3) or GCN4 of S. cerevisiae (4), respectively. Recently, homologous proteins were reported also for Aspergillus niger and Cryptonecria parasitica (5,6). In yeast, GCN2 plays a crucial role in signal perception and transduction.…”

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confidence: 97%

cpc-3, the Neurospora crassa Homologue of Yeast GCN2, Encodes a Polypeptide with Juxtaposed eIF2α Kinase and Histidyl-tRNA Synthetase-related Domains Required for General Amino Acid Control

Sattlegger¹,

Hinnebusch²,

Barthelmess³

1998

Journal of Biological Chemistry

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Based on characteristic amino acid sequences of kinases that phosphorylate the ␣ subunit of eukaryotic translation initiation factor 2 (eIF2␣ kinases), degenerate oligonucleotide primers were constructed and used to polymerase chain reaction-amplify from genomic DNA of Neurospora crassa a sequence encoding part of a putative protein kinase. With this sequence an open reading frame was identified encoding a predicted polypeptide with juxtaposed eIF2␣ kinase and histidyltRNA synthetase-related domains. The 1646 amino acid sequence of this gene, called cpc-3, showed 35% positional identity over almost the entire sequence with GCN2 of yeast, which stimulates translation of the transcriptional activator of amino acid biosynthetic genes encoded by GCN4. Strains disrupted for cpc-3 were unable to induce increased transcription and derepression of amino acid biosynthetic enzymes in amino acid-deprived cells. The cpc-3 mutation did not affect the ability to up-regulate mRNA levels of cpc-1, encoding the GCN4 homologue and transcriptional activator of amino acid biosynthetic genes in N. crassa, but the mutation abolished the dramatic increase of CPC1 protein level in response to amino acid deprivation. These findings suggest that cpc-3 is the functional homologue of GCN2, being required for increased translation of cpc-1 mRNA in amino acid-starved cells.

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Cloning and Characterization of a General Amino Acid Control Transcriptional Activator from the Chestnut Blight FungusCryphonectria parasitica

Cited by 28 publications

References 69 publications

Signal Transduction Cascades Regulating Fungal Development and Virulence

Signal Transduction Cascades Regulating Fungal Development and Virulence

Transcriptional Autoregulation and Inhibition of mRNA Translation of Amino Acid Regulator GenecpcAof Filamentous FungusAspergillus nidulans

cpc-3, the Neurospora crassa Homologue of Yeast GCN2, Encodes a Polypeptide with Juxtaposed eIF2α Kinase and Histidyl-tRNA Synthetase-related Domains Required for General Amino Acid Control

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