Abstract
Small heat shock proteins (sHSPs) are a group of chaperone proteins existed in all organisms. The functions of sHSPs in heat and abiotic stress responses in many glycophyte plants have been studied. However, their possible roles in halophyte plants are still largely known. In this work, a putative sHSP gene KvHSP26 was cloned from K. virginica. Bioinformatics analyses revealed that KvHSP26 encoded a chloroplastic protein with the typical features of sHSPs. Amino acid sequence alignment and phylogenetic analysis demonstrated that KvHSP26 shared 30%-77% homology with other sHSPs from Arabidopsis, cotton, durian, salvia, and soybean. Quantitative real-time PCR (qPCR) assays exhibited that KvHSP26 was constitutively expressed in different tissues such as leaves, stems, and roots, with a relatively higher expression in leaves. Furthermore, expression of KvHSP26 was strongly induced by salt, heat, osmotic stress, and ABA in K. virginica. All these results suggest that KvHSP26 encodes a new sHSP, which is involved in multiple abiotic stress responses in K. virginica, and it has a great potential to be used as a candidate gene for the breeding of plants with improved tolerances to various abiotic stresses.
Highlights
To cope with the adverse environmental conditions throughout their entire life cycle, plants have evolved a serial of sophisticated mechanisms [1, 2]
Our findings indicate that KvHSP26 could play an important role in the tolerance of K. virginica to different abiotic stresses
KvHSP26 encoded a 26.09 kDa protein consisting of 232 amino acids with a theoretical isoelectric point of 6.34 (Figure 1(a))
Summary
To cope with the adverse environmental conditions throughout their entire life cycle, plants have evolved a serial of sophisticated mechanisms [1, 2]. HSPs can bind directly to the denatured proteins to help their refolding and prevent their further aggregation and improve cell homeostasis under heat stress condition [4,5,6] Due to their high expression under heat stress condition, HSPs function as one of the most important kinds of chaperones in archaea, prokaryote, and eukaryote [7,8,9]. Based on their molecular weight, five HSP protein families have been identified: HSP20s/sHSPs, HSP60s, HSP70s, HSP90s, and HSP100s [10,11,12]. Different localizations of sHSPs indicate that they might have different functions in cells
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