Identification and Expression Analysis of Heat Shock Proteins in Wheat Infected with Powdery Mildew and Stripe Rust

AbstractHeat shock proteins (HSPs), which are encoded by conserved gene families in plants, are crucial for development and responses to diverse stresses. However, the wheat (Triticum aestivum) HSPs have not been systematically classified, especially those involved in protecting plants from disease. Here, we classified 119 DnaJ (Hsp40) proteins (TaDnaJs; encoded by 313 genes) and 41 Hsp70 proteins (TaHsp70s; encoded by 95 genes) into six and four groups, respectively, via a phylogenetic analysis. An examination of protein structures and a multiple sequence alignment revealed diversity in the TaDnaJ structural organization, but a highly conserved J-domain, which was usually characterized by an HPD motif followed by DRD or DED motifs. The expression profiles of these HSP-encoding homologous genes varied in response to Blumeria graminis f. sp. tritici and Puccinia striiformis f. sp. tritici. A quantitative real-time PCR analysis indicated a lack of similarity in the expression of DnaJ70b, Hsp70-30b, and Hsp90-4b in wheat infected by B. graminis f. sp. tritici, although the expression levels of these genes were abnormal in the infected resistant and susceptible lines. Furthermore, a direct interaction between DnaJ70 and TaHsp70-30 was not detected in a yeast two-hybrid assay. This study revealed the structure and expression profiles of the HSP-encoding genes in wheat. The resulting data may be useful for future functional analyses and for further elucidating the roles of wheat HSPs during responses to fungal infections.

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Wall-associated Receptor Kinase and The Expression Profiles in Wheat Responding to Fungal Stress

10.1101/2021.07.11.451968 ◽

2021 ◽

Author(s):

Hong Zhang ◽

Hanping Li ◽

Xiangyu Zhang ◽

Wenqian Yan ◽

Pingchuan Deng ◽

...

Keyword(s):

Puccinia Striiformis ◽

Fungal Infections ◽

Expression Profiles ◽

Puccinia Triticina ◽

Gene Families ◽

Triticum Aestivum L ◽

Pcr Analysis ◽

Homologous Genes ◽

Conserved Gene ◽

Encoding Genes

Cell wall-associated kinases (WAKs), which are encoded by conserved gene families in plants, are crucial for development and responses to diverse stresses. However, the wheat (Triticum aestivum L.) WAKs have not been systematically classified, especially those involved in protecting plants from disease. Here, we classified 129 WAK proteins (encoded by 232 genes) and 75 WAK-Like proteins (WAKLs; encoded by 109 genes) into four groups, via a phylogenetic analysis. An examination of protein sequence alignment revealed diversity in the GUB-domain of WAKs structural organization, but it was usually characterized by a PYPFG motif followed by CxGxGCC motifs, while the EGF-domain was usually initiated with a YAC motif, and eight cysteine residues were spliced by GNPY motif. The expression profiles of WAK-encoding homologous genes varied in response to Blumeria graminis f. sp. tritici (Bgt), Puccinia striiformis f. sp. tritici (Pst) and Puccinia triticina (Pt) stress. A quantitative real-time polymerase chain reaction (qRT-PCR) analysis proved that TaWAK75 and TaWAK76b were involved in wheat resistance to Bgt. This study revealed the structure of the WAK-encoding genes in wheat, which may be useful for future functional elucidation of wheat WAKs responses to fungal infections.

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An in silico analysis of genome-wide expression profiles of the effects of exhaustive exercise identifies heat shock proteins as the key players

Meta Gene ◽

10.1016/j.mgene.2022.101012 ◽

2022 ◽

pp. 101012

Author(s):

Carlos A. Orozco ◽

Yeimy González-Giraldo ◽

Diego A. Bonilla ◽

Diego A. Forero

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

In Silico ◽

Expression Profiles ◽

In Silico Analysis ◽

Genome Wide ◽

Key Players ◽

Shock Proteins ◽

Genome Wide Expression ◽

Silico Analysis

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Characterizing Gene Copy Number of Heat Shock Protein Gene Families in the Emerald Rockcod, Trematomus bernacchii

Genes ◽

10.3390/genes11080867 ◽

2020 ◽

Vol 11 (8) ◽

pp. 867

Author(s):

Anthony D. Tercero ◽

Sean P. Place

Keyword(s):

Heat Shock ◽

Gene Duplication ◽

Heat Shock Proteins ◽

Heat Shock Response ◽

Copy Number ◽

Gene Families ◽

Gene Copy ◽

Shock Response ◽

Trematomus Bernacchii ◽

Shock Proteins

The suborder Notothenioidae is comprised of Antarctic fishes, several of which have lost their ability to rapidly upregulate heat shock proteins in response to thermal stress, instead adopting a pattern of expression resembling constitutive genes. Given the cold-denaturing effect that sub-zero waters have on proteins, evolution in the Southern Ocean has likely selected for increased expression of molecular chaperones. These selective pressures may have also enabled retention of gene duplicates, bolstering quantitative output of cytosolic heat shock proteins (HSPs). Given that newly duplicated genes are under more relaxed selection, it is plausible that gene duplication enabled altered regulation of such highly conserved genes. To test for evidence of gene duplication, copy number of various isoforms within major heat shock gene families were characterized via qPCR and compared between the Antarctic notothen, Trematomus bernacchii, which lost the inducible heat shock response, and the non-Antarctic notothen, Notothenia angustata, which maintains an inducible heat shock response. The results indicate duplication of isoforms within the hsp70 and hsp40 super families have occurred in the genome of T. bernacchii. The findings suggest gene duplications may have been critical in maintaining protein folding efficiency in the sub-zero waters and provided an evolutionary mechanism of alternative regulation of these conserved gene families.

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mRNA expression profiles of heat shock proteins of wild and salinity-tolerant swimming crabs, Portunus trituberculatus, subjected to low salinity stress

Genetics and Molecular Research ◽

10.4238/2014.august.29.5 ◽

2014 ◽

Vol 13 (3) ◽

pp. 6837-6847 ◽

Cited By ~ 5

Author(s):

X.N. Bao ◽

C.K. Mu ◽

C. Zhang ◽

Y.F. Wang ◽

W.W. Song ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Mrna Expression ◽

Salinity Stress ◽

Expression Profiles ◽

Portunus Trituberculatus ◽

Low Salinity ◽

Shock Proteins ◽

Swimming Crabs

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Genome-wide identification and classification of the Hsf and sHsp gene families in Prunus mume, and transcriptional analysis under heat stress

PeerJ ◽

10.7717/peerj.7312 ◽

2019 ◽

Vol 7 ◽

pp. e7312 ◽

Cited By ~ 5

Author(s):

Xueli Wan ◽

Jie Yang ◽

Cong Guo ◽

Manzhu Bao ◽

Junwei Zhang

Keyword(s):

Heat Stress ◽

Heat Shock ◽

Transcriptional Activation ◽

Gene Families ◽

Transcriptional Analysis ◽

Pcr Analysis ◽

Prunus Mume ◽

Reverse Transcription Pcr ◽

Shsp Gene ◽

Shock Proteins

The transcriptional activation of heat shock proteins (Hsps) by heat shock transcription factors (Hsfs) is presumed to have a pivotal role in plant heat stress (HS) response. Prunus mume is an ornamental woody plant with distinctive features, including rich varieties and colors. In this study, 18 Hsfs and 24 small Hsps (sHsps) were identified in P. mume. Their chromosomal locations, protein domains, conserved motifs, phylogenetic relationships, and exon–intron structures were analyzed and compared with Arabidopsis thaliana Hsfs or sHsps. A total of 18 PmHsf members were classified into three major classes, A, B, and C. A total of 24 PmsHsps were grouped into eight subfamilies (CI to CIII, P, endoplasmic reticulum, M, and CI- or P-related). Quantitative reverse transcription PCR analysis revealed that members of the A2, A7, and A9 groups became the prominent Hsfs after heat shock, suggesting their involvement in a key regulatory role of heat tolerance. Most of the PmsHsp genes were up-regulated upon exposure to HS. Overall, our data contribute to an improved understanding of the complexity of the P. mume Hsf and sHsp gene families, and provide a basis for directing future systematic studies investigating the roles of the Hsf and sHsp gene families.

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Cross-Omics Comparison of Stress Responses in Mesothelial Cells Exposed to Heat- versus Filter-Sterilized Peritoneal Dialysis Fluids

BioMed Research International ◽

10.1155/2015/628158 ◽

2015 ◽

Vol 2015 ◽

pp. 1-12 ◽

Cited By ~ 4

Author(s):

Klaus Kratochwill ◽

Thorsten O. Bender ◽

Anton M. Lichtenauer ◽

Rebecca Herzog ◽

Silvia Tarantino ◽

...

Keyword(s):

Peritoneal Dialysis ◽

Heat Shock ◽

Heat Shock Proteins ◽

Protein Expression ◽

Stress Responses ◽

Expression Profiles ◽

Mrna Level ◽

Mesothelial Cells ◽

Peritoneal Mesothelial Cells ◽

Shock Proteins

Recent research suggests that cytoprotective responses, such as expression of heat-shock proteins, might be inadequately induced in mesothelial cells by heat-sterilized peritoneal dialysis (PD) fluids. This study compares transcriptome data and multiple protein expression profiles for providing new insight into regulatory mechanisms. Two-dimensional difference gel electrophoresis (2D-DIGE) based proteomics and topic defined gene expression microarray-based transcriptomics techniques were used to evaluate stress responses in human omental peritoneal mesothelial cells in response to heat- or filter-sterilized PD fluids. Data from selected heat-shock proteins were validated by 2D western-blot analysis. Comparison of proteomics and transcriptomics data discriminated differentially regulated protein abundance into groups depending on correlating or noncorrelating transcripts. Inadequate abundance of several heat-shock proteins following exposure to heat-sterilized PD fluids is not reflected on the mRNA level indicating interference beyond transcriptional regulation. For the first time, this study describes evidence for posttranscriptional inadequacy of heat-shock protein expression by heat-sterilized PD fluids as a novel cytotoxic property. Cross-omics technologies introduce a novel way of understanding PDF bioincompatibility and searching for new interventions to reestablish adequate cytoprotective responses.

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