Abstract

BackgroundHeat shock proteins have important functions in regulating plant growth and response to abiotic stress. HSP70 family genes have been described in several plant species, but a comprehensive analysis of the HSP70 family genes in cabbage has not been reported to date, especially their roles in floral development.ResultsIn this study, we identified 52 BoHSP70 genes in cabbage. The gene structures, motifs, and chromosome locations of the BoHSP70 genes were analyzed. The genes were divided into seven classes using a phylogenetic analysis. An expression analysis showed that the BoHSP70 genes were highly expressed in actively growing tissues, including buds and calluses. In addition, six BoHSP70 genes were highly expressed in the binuclear-pollen-stage buds of a male fertile line compared with its near isogenic sterile line. These results were further verified using qRT-PCR. Subcellular localization analysis of the bud-specific gene BoHSP70–5 showed that it was localized in the cytoplasm.ConclusionsOur results help to elucidate the involvement of the BoHSP70 family genes in cabbage floral development and establish the groundwork for future research on the functions of these genes.

Highlights

  • Heat shock proteins have important functions in regulating plant growth and response to abiotic stress

  • Forty of the BoHSP70 genes were distributed on all nine chromosomes with chromosomes 1 and 3 harboring the most BoHSP70 genes

  • Our results indicated that all the values were less than 1, indicating that the BoHSP70 genes primarily evolved under the influence of purifying selection (Table 2)

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Summary

Introduction

Heat shock proteins have important functions in regulating plant growth and response to abiotic stress. HSP70, a type of heat shock protein (HSP), has long been recognized as one of the most conserved protein families, which can respond to external environmental stimuli and improve the ability of the organism to adjust to an adverse environment [1,2,3]. HSP70s function as molecular chaperones, presumably by protecting proteins against aggregation based on their ability to bind to hydrophobic amino acid residues or surfaces that are exposed by proteins in nonnative states. The heat shock protein accounts for approximately 5% of the total cellular protein, Many studies have shown that HSP70 is closely related to plant abiotic stress [10], disease resistance [11], and growth and development [12].

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