scholarly journals Analysis of TabZIP15 transcription factor from Trichoderma asperellum ACCC30536 and its function under pathogenic toxin stress

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Zeyang Yu ◽  
Zhiying Wang ◽  
Yuzhou Zhang ◽  
Yucheng Wang ◽  
Zhihua Liu
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Leucine Zipper ◽  
Differential Expression Analysis ◽  
Trichoderma Asperellum ◽  
Nutrient Competition ◽  
Gene Encoding ◽  
Cytospora Chrysosperma ◽  
Minimal Media ◽  
Basic Region

Abstract The TabZIP15 gene encoding a 396 amino acid (aa) polypeptide in the fungus Trichoderma asperellum ACCC30536 was cloned and characterised. The protein includes a basic region motif (NR-x2-QR-x2-R) and has a pillar-like structure. The 25 basic region/leucine zipper transcription factors (TFs) identified in the T. asperellum genome were divided into YAP (14 TFs), ATF2 (5), GCN4 (2), Zip1 (2), BRLZ (1) and u1 (1) subfamilies based on conserved domains. T. asperellum was cultured in minimal media (MM) control, C-Hungry and N-Hungry medium (to simulate nutrient competition and interaction with pathogens, respectively), and differential expression analysis showed that 14 TabZIP genes (including TabZIP15) were significantly altered under both conditions; TabZIP23 responded strongly to N-Hungry media and TabZIP24 responded strongly to C-Hungry media. However, only YAP genes TabZIP15, TabZIP12 and TabZIP2 were significantly upregulated under both conditions, and expression levels of TabZIP15 were highest. T. asperellum was also cultured in the presence of five fungal pathogenic toxins, and RT-qPCR results showed that TabZIP15 was significantly upregulated in four of the five toxin stress conditions (MM + Rhizoctonia solani, MM + Fusarium oxysporum, MM + Alternaria alternata and MM + Cytospora chrysosperma).

scholarly journals Expression of Adhesive Pili and the Collagen-Binding Adhesin Ace Is Activated by ArgR Family Transcription Factors inEnterococcus faecalis

2018 ◽  
Vol 200 (18) ◽  
Author(s):  
Dawn A. Manias ◽  
Gary M. Dunny
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Enterococcus Faecalis ◽  
Opportunistic Infections ◽  
Structural Genes ◽  
Gene Encoding ◽  
Collagen Binding ◽  
Content Type ◽  
Surface Adhesins

ABSTRACTIt was shown previously that the disruption of theahrCgene encoding a predicted ArgR family transcription factor results in a severe defect in biofilm formationin vitro, as well as a significant attenuation of virulence ofEnterococcus faecalisstrain OG1RF in multiple experimental infection models. Using transcriptome sequencing (RNA-seq), we observedahrC-dependent changes in the expression of more than 20 genes. AhrC-repressed genes included predicted determinants of arginine catabolism and several other metabolic genes and predicted transporters, while AhrC-activated genes included determinants involved in the production of surface protein adhesins. Most notably, the structural and regulatory genes of theebplocus encoding adhesive pili were positively regulated, as well as theacegene, encoding a collagen-binding adhesin. UsinglacZtranscription reporter fusions, we determined thatahrCand a secondargRtranscription factor gene,argR2, both function to activate the expression ofebpR, which directly activates the transcription of the pilus structural genes. Our data suggest that in the wild-typeE. faecalis, the low levels of EbpR limit the expression of pili and that biofilm biomass is also limited by the amount of pili expressed by the bacteria. The expression ofaceis similarly enhanced by AhrC and ArgR2, butaceexpression is not dependent on EbpR. Our results demonstrate the existence of novel regulatory cascades controlled by a pair of ArgR family transcription factors that might function as a heteromeric protein complex.IMPORTANCECell surface adhesins play critical roles in the formation of biofilms, host colonization, and the pathogenesis of opportunistic infections byEnterococcus faecalis. Here, we present new results showing that the expression of two major enterococcal surface adhesins,ebppili, and the collagen-binding protein Ace is positively regulated at the transcription level by twoargRfamily transcription factors, AhrC and ArgR2. In the case of pili, the direct target of regulation is theebpRgene, previously shown to activate the transcription of the pilus structural genes, while the activation ofacetranscription appears to be directly impacted by the two ArgR proteins. These transcription factors may represent new targets for blocking enterococcal infections.

scholarly journals Phosphorylation of MafA Is Essential for Its Transcriptional and Biological Properties

2001 ◽  
Vol 21 (14) ◽  
pp. 4441-4452 ◽  
Author(s):  
Sofia Benkhelifa ◽  
Sylvain Provot ◽  
Eugène Nabais ◽  
Alain Eychène ◽  
Georges Calothy ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcriptional Activity ◽  
Leucine Zipper ◽  
Biological Properties ◽  
Erk Pathway ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Basic Region

ABSTRACT We previously described the identification of quail MafA, a novel transcription factor of the Maf bZIP (basic region leucine zipper) family, expressed in the differentiating neuroretina (NR). In the present study, we provide the first evidence that MafA is phosphorylated and that its biological properties strongly rely upon phosphorylation of serines 14 and 65, two residues located in the transcriptional activating domain within a consensus for phosphorylation by mitogen-activated protein kinases and which are conserved among Maf proteins. These residues are phosphorylated by ERK2 but not by p38, JNK, and ERK5 in vitro. However, the contribution of the MEK/ERK pathway to MafA phosphorylation in vivo appears to be moderate, implicating another kinase. The integrity of serine 14 and serine 65 residues is required for transcriptional activity, since their mutation into alanine severely impairs MafA capacity to activate transcription. Furthermore, we show that the MafA S14A/S65A mutant displays reduced capacity to induce expression of QR1, an NR-specific target of Maf proteins. Likewise, the integrity of serines 14 and 65 is essential for the MafA ability to stimulate expression of crystallin genes in NR cells and to induce NR-to-lens transdifferentiation. Thus, the MafA capacity to induce differentiation programs is dependent on its phosphorylation.

scholarly journals Redox-mediated Mechanisms Regulate DNA Binding Activity of the G-group of Basic Region Leucine Zipper (bZIP) Transcription Factors inArabidopsis

2012 ◽  
Vol 287 (33) ◽  
pp. 27510-27525 ◽  
Author(s):  
Jehad Shaikhali ◽  
Louise Norén ◽  
Juan de Dios Barajas-López ◽  
Vaibhav Srivastava ◽  
Janine König ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Leucine Zipper ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Bzip Transcription Factors ◽  
Basic Region

Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP

2005 ◽  
Vol 386 (9) ◽  
Author(s):  
Jude Al Sarraj ◽  
Charles Vinson ◽  
Gerald Thiel
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Gene Transcription ◽  
Leucine Zipper ◽  
Nutrient Sensing ◽  
Asparagine Synthetase ◽  
Nutrient Deprivation ◽  
Amino Acid Deprivation ◽  
Response Unit ◽  
Basic Region

AbstractAsparagine synthetase catalyses the glutamine- and ATP-dependent conversion of aspartic acid to asparagine. In human hepatoma cells cultured in mediumcontaining amino acids, the mRNA of asparagine synthetase is not detectable by RNase protection mapping. However, maintaining the cells in amino acid-free Krebs-Ringer bicarbonate buffer strongly upregulated asparagine synthetase biosynthesis. The effect of amino acid deprivation on asparagine synthetase gene transcription is mediated by a genetic element termed the nutrient-sensing response unit. Previous studies revealed that the basic region leucine zipper (bZIP) transcription factor CREB2/ATF4 is involved in the nutrient deprivation-induced upregulation of asparagine synthetase gene transcription. Here we show that overexpression of the bZIP protein ATF5, a transcriptional activator, stimulates asparagine synthetase promoter/reporter gene transcription via the nutrient-sensing response unit. In contrast, ATF5 does not transactivate cAMP response element (CRE)-containing reporter genes. Overexpression of the C/EBP homologous transcription factor CHOP impaired transcriptional activation of the asparagine synthetase promoter following amino acid deprivation or over-expression of ATF5 or CREB2/ATF4. These data indicate that CHOP functions as a shut-off-device for nutrient deprivation-induced gene transcription.

scholarly journals Sucrose-induced translational repression of plant bZIP-type transcription factors

2005 ◽  
Vol 33 (1) ◽  
pp. 272-275 ◽  
Author(s):  
A. Wiese ◽  
N. Elzinga ◽  
B. Wobbes ◽  
S. Smeekens
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Translational Control ◽  
Leucine Zipper ◽  
Upstream Open Reading Frame ◽  
Bzip Transcription Factor ◽  
Reading Frame ◽  
Signalling Molecules ◽  
Transcription Factor Genes ◽  
Plant Genes

Sugars as signalling molecules exert control on the transcription of many plant genes. Sugar signals also alter mRNA and protein stability. Increased sucrose concentrations specifically repress translation of the S-class basic region leucine zipper (bZIP) type transcription factor AtbZIP11/ATB2. This sucrose-induced repression of translation (SIRT) depends on translation of a highly conserved upstream open reading frame (uORF) in the 5′ UTR of the gene. This conserved uORF is exclusively encoded in 5′ UTRs of several plant S-class bZIP transcription factors. Arabidopsis homologues of ATB2/AtbZIP11, which harbour the conserved uORF, also show SIRT. Therefore, SIRT emerges as a general sucrose translational control mechanism of a group of transcription factors. SIRT might be part of a sucrose-specific signalling pathway, controlling expression of plant bZIP transcription factor genes.

scholarly journals BHLHE40, a third transcription factor required for insulin induction of SREBP-1c mRNA in rodent liver

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Jing Tian ◽  
Jiaxi Wu ◽  
Xiang Chen ◽  
Tong Guo ◽  
Zhijian J Chen ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Fatty Acid ◽  
Fatty Liver ◽  
Fatty Acid Synthesis ◽  
Gene Knockout ◽  
Rat Hepatocytes ◽  
Acid Synthesis ◽  
Gene Encoding ◽  
Fasted Rats

In obesity, elevated insulin causes fatty liver by activating the gene encoding SREBP-1c, a transcription factor that enhances fatty acid synthesis. Two transcription factors, LXRα and C/EBPβ, are necessary but not sufficient for insulin induction of hepatic SREBP-1c mRNA. Here, we show that a third transcription factor, BHLHE40, is required. Immunoprecipitation revealed that BHLHE40 binds to C/EBPβ and LXRα in livers of rats that had fasted and then refed. Hepatic BHLHE40 mRNA rises rapidly when fasted rats are refed and when rat hepatocytes are incubated with insulin. Preventing this rise by gene knockout in mice or siRNAs in hepatocytes reduces the insulin-induced rise in SREBP-1c mRNA. Although BHLHE40 is necessary for insulin induction of SREBP-1c, it is not sufficient as demonstrated by failure of lentiviral BHLHE40 overexpression to increase hepatocyte SREBP-1c mRNA in the absence of insulin. Thus, an additional event is required for insulin to increase SREBP-1c mRNA.

scholarly journals Mechanism of conditional partner selectivity in MITF/TFE family transcription factors with a conserved coiled coil stammer motif

2019 ◽  
Vol 48 (2) ◽  
pp. 934-948 ◽  
Author(s):  
Vivian Pogenberg ◽  
Josué Ballesteros-Álvarez ◽  
Romana Schober ◽  
Ingibjörg Sigvaldadóttir ◽  
Agnieszka Obarska-Kosinska ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
High Resolution ◽  
Nuclear Localization ◽  
Leucine Zipper ◽  
Coiled Coil ◽  
Fundamental Difference ◽  
Wild Type ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix

Abstract Interrupted dimeric coiled coil segments are found in a broad range of proteins and generally confer selective functional properties such as binding to specific ligands. However, there is only one documented case of a basic-helix–loop–helix leucine zipper transcription factor—microphthalmia-associated transcription factor (MITF)—in which an insertion of a three-residue stammer serves as a determinant of conditional partner selectivity. To unravel the molecular principles of this selectivity, we have analyzed the high-resolution structures of stammer-containing MITF and an engineered stammer-less MITF variant, which comprises an uninterrupted symmetric coiled coil. Despite this fundamental difference, both MITF structures reveal identical flanking in-phase coiled coil arrangements, gained by helical over-winding and local asymmetry in wild-type MITF across the stammer region. These conserved structural properties allow the maintenance of a proper functional readout in terms of nuclear localization and binding to specific DNA-response motifs regardless of the presence of the stammer. By contrast, MITF heterodimer formation with other bHLH-Zip transcription factors is only permissive when both factors contain either the same type of inserted stammer or no insert. Our data illustrate a unique principle of conditional partner selectivity within the wide arsenal of transcription factors with specific partner-dependent functional readouts.

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