HSP70 gene expression responses to the temperature stress in pufferfish (Takifugu rubripes)

2021 ◽  
Author(s):  
Kun-peng Fan ◽  
Xin-tong Hua ◽  
Ya-fang Liu ◽  
Zhi-qiang Zhang ◽  
Xiao-hao Li ◽  
...  
Keyword(s):  
Gene Expression ◽  
Physiological Function ◽  
Specific Gene ◽  
Takifugu Rubripes ◽  
High Similarity ◽  
Coping With Stress ◽  
Reading Frame ◽  
And Coping ◽  
Experimental Group ◽  
Normal Physiological Function

Abstract In this study, we isolated and characterized HSP70 cDNA from pufferfish (Takifugu rubripes). The 3,053 bp full-length TrHSP70 sequence consisted of a 167 bp 5′-UTR (untranslated region), a 2,535 bp ORF (open reading frame), and a 351 bp 3′-UTR. BLAST analysis revealed that the TrHSP70 shared high similarity with HSP70 sequences in other species. In our study, we set three experimental groups as H1 group (20 °C), H2 group (24 °C) and H3 group (28 °C) for checking expression level of TrHSP70 in T. rubripes. Tissues specific gene expression results showed that TrHSP70 had higher expression in the intestines than other tissues of the T. rubripes by RT-qPCR. In the experimental group, we found that the expression of TrHSP70 was upregulated in different tissues in H3 group. The results show that TrHSP70 is a constitutively expressed gene, which plays an important role in maintaining normal physiological function and coping with stress

scholarly journals The Transcription Factor Xrp1 is Required for PERK-Mediated Antioxidant Gene Induction in Drosophila

2021 ◽  
Author(s):  
Brian Brown ◽  
Sahana Mitra ◽  
Finnegan D Roach ◽  
Deepika Vasudevan ◽  
Hyung Don Ryoo
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Upstream Open Reading Frame ◽  
Bzip Transcription Factor ◽  
Specific Gene ◽  
Antioxidant Genes ◽  
Reading Frame ◽  
Protein Levels ◽  
Signaling Axis ◽  
The Unfolded Protein Response

PERK is an endoplasmic reticulum (ER) transmembrane sensor that phosphorylates eIF2a to initiate the Unfolded Protein Response (UPR). eIF2a phosphorylation promotes stress-responsive gene expression most notably through the transcription factor ATF4 that contains a regulatory 5′ leader. Possible PERK effectors other than ATF4 remain poorly understood. Here, we report that the bZIP transcription factor Xrp1 is required for ATF4-independent PERK signaling. Cell type-specific gene expression profiling in Drosophila indicated that delta-family glutathione-S-transferases (gstD) are prominently induced by the UPR-activating transgene Rh1G69D. Perk was necessary and sufficient for such gstD induction, but ATF4 was not required. Instead, Perk and other regulators of eIF2a phosphorylation regulated Xrp1 protein levels to induce gstDs. The Xrp1 5′ leader has a conserved upstream Open Reading Frame (uORF) analogous to those that regulate ATF4 translation. The gstD-GFP reporter induction required putative Xrp1 binding sites. These results indicate that antioxidant genes are highly induced by a previously unrecognized UPR signaling axis consisting of PERK and Xrp1.

Cloning and characterization of theddsAgene encoding decaprenyl diphosphate synthase fromRhodobacter capsulatusB10

2006 ◽  
Vol 52 (12) ◽  
pp. 1141-1147 ◽  
Author(s):  
Xinyi Liu ◽  
Haizhen Wu ◽  
Jiang Ye ◽  
Qinsheng Yuan ◽  
Huizhan Zhang
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Rhodobacter Capsulatus ◽  
Open Reading Frame ◽  
High Similarity ◽  
Reading Frame ◽  
Endogenous Production ◽  
Genome Library

A decaprenyl diphosphate synthase gene (ddsA, GenBank accession No. DQ191802) was cloned from Rhodobacter capsulatus B10 by constructing and screening the genome library. An open reading frame of 1002 bp was revealed from sequence analysis. The deduced polypeptide consisted of 333 amino acids residues with an molecular mass of about 37 kDa. The DdsA protein contained the conserved amino acid sequence (DDXXD) of E-type polyprenyl diphosphate synthase and showed high similarity to others. In contrast, DdsA showed only 39% identity to a solanesyl diphosphate synthase cloned from R. capsulatus SB1003. DdsA was expressed successfully in Escherichia coli. Assaying the enzyme in vivo found it made E.coli synthesize UQ-10 in addition to the endogenous production UQ-8.Key words: ubiquinone, polyprenyl diphosphate synthase, gene expression, Rhodobacter capsulatus.

scholarly journals The transcription factor Xrp1 is required for PERK-mediated antioxidant gene induction in Drosophila

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Brian Brown ◽  
Sahana Mitra ◽  
Finnegan D Roach ◽  
Deepika Vasudevan ◽  
Hyung Don Ryoo
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Upstream Open Reading Frame ◽  
Bzip Transcription Factor ◽  
Specific Gene ◽  
Antioxidant Genes ◽  
Reading Frame ◽  
Protein Levels ◽  
Eif2α Phosphorylation ◽  
The Unfolded Protein Response

PERK is an endoplasmic reticulum (ER) transmembrane sensor that phosphorylates eIF2α to initiate the Unfolded Protein Response (UPR). eIF2α phosphorylation promotes stress-responsive gene expression most notably through the transcription factor ATF4 that contains a regulatory 5’ leader. Possible PERK effectors other than ATF4 remain poorly understood. Here, we report that the bZIP transcription factor Xrp1 is required for ATF4-independent PERK signaling. Cell-type-specific gene expression profiling in Drosophila indicated that delta-family glutathione-S-transferases (gstD) are prominently induced by the UPR-activating transgene Rh1G69D. Perk was necessary and sufficient for such gstD induction, but ATF4 was not required. Instead, Perk and other regulators of eIF2α phosphorylation regulated Xrp1 protein levels to induce gstDs. The Xrp1 5’ leader has a conserved upstream Open Reading Frame (uORF) analogous to those that regulate ATF4 translation. The gstD-GFP reporter induction required putative Xrp1 binding sites. These results indicate that antioxidant genes are highly induced by a previously unrecognized UPR signaling axis consisting of PERK and Xrp1.

scholarly journals The Gene ssl3076 Encodes a Protein Mediating the Salt-Induced Expression of ggpS for the Biosynthesis of the Compatible Solute Glucosylglycerol in Synechocystis sp. Strain PCC 6803

2010 ◽  
Vol 192 (17) ◽  
pp. 4403-4412 ◽  
Author(s):  
Stephan Klähn ◽  
Antje Höhne ◽  
Elke Simon ◽  
Martin Hagemann
Keyword(s):  
Gene Expression ◽  
Reporter Gene ◽  
Transcriptional Start Site ◽  
Gene Promoter ◽  
Compatible Solute ◽  
Negative Regulator ◽  
Specific Gene ◽  
Reading Frame ◽  
Low Salt ◽  
Pcc 6803

ABSTRACT Acclimation to high salt concentrations involves concerted changes in gene expression. For the majority of salt-regulated genes, the mechanism underlying the induction process is not known. The gene ggpS (sll1566), which encodes the glucosylglycerol-phosphate synthase responsible for the synthesis of the compatible solute glucosylglycerol (GG), is specifically induced by salt in the cyanobacterial model strain Synechocystis sp. strain PCC 6803. To identify mechanisms mediating this salt-specific gene regulation, the ggpS promoter was analyzed in more detail. 5′ rapid amplification of cDNA ends (5′-RACE) experiments revealed that the adjacent open reading frame (ORF), which is annotated as unknown protein Ssl3076, overlaps with the transcriptional start site of the ggpS gene. Reporter gene expression analyses indicated an essential role for the intact ssl3076 gene in the salt-regulated transcription of a gfp reporter gene. Promoter fragments containing a mutated ssl3076 lost the salt regulation; similarly, a frameshift mutation in ssl3076 resulted in a high level of ggpS expression under low-salt conditions, thereby establishing this small ORF, named ggpR, as a negative regulator of ggpS. Interestingly, small ORFs were also found adjacent to ggpS genes in the genomes of other GG-accumulating cyanobacteria. These results suggest that the GgpR protein represses ggpS expression under low-salt conditions, whereas in salt-shocked and salt-acclimated cells a stress-proportional ggpS expression occurs, leading to GG accumulation.

Sign in / Sign up

Export Citation Format

Share Document