Abstract

In this work, the involvement of heat shock proteins (HSP70) in barley (Hordeum vulgare) has been studied in response to drought and salinity. Thus, 3 barley genotypes usually cultivated and/or selected in Italy, 3 Middle East/North Africa landraces and genotypes and 1 improved genotype from ICARDA have been studied to identify those varieties showing the best stress response. Preliminarily, a bioinformatic characterization of the HSP70s protein family in barley has been made by using annotated Arabidopsis protein sequences. This study identified 20 putative HSP70s orthologs in the barley genome. The construction of un-rooted phylogenetic trees showed the partition into four main branches, and multiple subcellular localizations. The enhanced HSP70s presence upon salt and drought stress was investigated by both immunoblotting and expression analyses. It is worth noting the Northern Africa landraces showed peculiar tolerance behavior versus drought and salt stresses. The drought and salinity conditions indicated the involvement of specific HSP70s to counteract abiotic stress. Particularly, the expression of cytosolic MLOC_67581, mitochondrial MLOC_50972, and encoding for HSP70 isoforms showed different expressions and occurrence upon stress. Therefore, genotypes originated in the semi-arid area of the Mediterranean area can represent an important genetic source for the improvement of commonly cultivated high-yielding varieties.

Highlights

  • The Heat Shock Proteins 70 (HSP70s) are a subfamily of the heat shock proteins, a well-known class of molecular chaperons involved in an abiotic stress response [1]

  • The HSP70s act on misfolded and truncated proteins protecting the cells and the tissues [11,12]. This mechanism is regulated by heat shock factors (Hsfs), a group of transcription factors regulating HSP70s expression [12,13]

  • In European countries such as Germany, France, UK, value of barley highlight the need of select new genotypes with improved tolerance to abiotic stress

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Summary

Introduction

The Heat Shock Proteins 70 (HSP70s) are a subfamily of the heat shock proteins, a well-known class of molecular chaperons involved in an abiotic stress response [1]. The HSP70s present a nucleotide binding domain (NBD) of 45kDa showing ATPase activity and a 15 kDa substrate binding domain (SBD) with a C-terminal domain covering the SBD [2]. A plants’ HSP70s show several different subcellular localizations, namely cytosolic, nuclear, endoplasmic reticulum, chloroplastic and mitochondrial [7,8]. The HSP70s act on misfolded and truncated proteins protecting the cells and the tissues [11,12]. This mechanism is regulated by heat shock factors (Hsfs), a group of transcription factors regulating HSP70s expression [12,13]

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