Abstract
Heat-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 L.) 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 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 HSP-encoding homologous genes varied in response to Blumeria graminis f. sp. tritici (Bgt) and Puccinia striiformis f. sp. tritici (Pst) stress. A quantitative real-time polymerase chain reaction (qRT-PCR) analysis indicated a lack of similarity in the expression of DnaJ70b, Hsp70-30b, and Hsp90-4b in Bgt-infected resistant and susceptible wheat. Furthermore, a direct interaction between DnaJ70 and TaHsp70-30 was not detected in a yeast two-hybrid (Y2H) assay, but screening cDNA library and Y2H evidence supported that TaHsp70-30 not only interacts directly with heat-shock transcription factor (HSF) A9-like protein but also interacts with TaHsp90-4 by HSP organizing protein. This study revealed the structure and expression profiles of the HSP-encoding genes in wheat, which may be useful for future functional elucidation of wheat HSPs responses to fungal infections.
Highlights
In the cytoplasm and nucleus, the heat shock response mediates stress-induced transcriptional changes via the increased production of essential protective factors [1] called heat shock proteins (HSPs; known as molecular chaperones) [2]
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, the expression levels of these genes were abnormal in the infected resistant and susceptible lines
Screening the PmAs846 physical map, with the Chinese Spring wheat genome used as a reference sequence, indicated that TraesCS5B02G374900 is located between the cosegregation markers BJ261635 with XFCP620 flanking PmAS846 [32]
Summary
In the cytoplasm and nucleus, the heat shock response mediates stress-induced transcriptional changes via the increased production of essential protective factors [1] called heat shock proteins (HSPs; known as molecular chaperones) [2]. Hsp functions cooperatively with the highly conserved Hsp via co-chaperones [11, 12], resulting in the assembly, maturation, stabilization, and activation of key signalling proteins, including protein kinases and transcription factors in eukaryotic cells [13, 14]. These observations suggest there is an important cycle of functions related to the interaction between Hsp and the J-domain proteins Hsp and Hsp90 [15, 16]. The Hsp molecular chaperone ensures proteins are maintained in their active conformations [17]
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