HSP70 from the Antarctic sea urchin Sterechinus neumayeri: molecular characterization and expression in response to heat stress

Abstract

BackgroundHeat stress proteins are implicated in stabilizing and refolding denatured proteins in vertebrates and invertebrates. Members of the Hsp70 gene family comprise the cognate heat shock protein (Hsc70) and inducible heat shock protein (Hsp70). However, the cDNA sequence and the expression of Hsp70 in the Antarctic sea urchin are unknown.MethodsWe amplified and cloned a transcript sequence of 1991 bp from the Antarctic sea urchin Sterechinus neumayeri, experimentally exposed to heat stress (5 and 10 °C for 1, 24 and 48 h). RACE-PCR and qPCR were employed to determine Hsp70 gene expression, while western blot and ELISA methods were used to determine protein expression.ResultsThe sequence obtained from S. neumayeri showed high identity with Hsp70 members. Several Hsp70 family features were identified in the deduced amino acid sequence and they indicate that the isolated Hsp70 is related to the cognate heat shock protein type. The corresponding 70 kDa protein, called Sn-Hsp70, was immune detected in the coelomocytes and the digestive tract of S. neumayeri using a monospecific polyclonal antibody. We showed that S. neumayeri do not respond to acute heat stress by up-regulation of Sn-Hsp70 at transcript and protein level. Furthermore, the Sn-Hsp70 protein expression was not induced in the digestive tract.ConclusionsOur results provide the first molecular evidence that Sn-Hsp70 is expressed constitutively and is non-induced by heat stress in S. neumayeri.

Characterization of Inducible HSP70 Genes in an Antarctic Yeast, Glaciozyma antarctica PI12, in Response to Thermal Stress

“…This study is the first description of the gene expression of HSP70 chaperones of the Antarctic obligate psychrophilic yeast, G. antarctica PI12, during conditions of acute thermal stress and cold shock. To date, several investigations on Antarctic organisms have evaluated the thermal stress response related to the expression of Hsp70 at different temperatures [26][27][28][29][42][43][44][45]. However, in Antarctic yeast, the expression of type HSP70 chaperones has not yet been evaluated.…”

“…Several related studies on G. antarctica PI12 have provided some insight into the strategies used by this yeast to adapt to thermal stress [19][20][21][22][23]. Most stress-related gene studies have been carried out at the gene level, and our understanding of the molecular architecture of the proteins is still limited [5][6][7]9,13,17,[24][25][26][27][28][29]. In the previous study by , a total of five Hsp70s were found to have significant expression patterns in response to heat stress [23].…”

Prospecting Biomarkers for Diagnostic and Therapeutic Approaches in Pythiosis

“…Among the seven matching spots, the protein identification revealed heat-shock cognate 70 KDa protein (Hsc 70), heat-shock 70 KDa protein (Hsp 70), glucan 1,3-betaglucosidase, fructose-bisphosphate aldolase, aconitate hydratase, and serine/threonineprotein phosphatase,14-3-3 protein epsilon. Heat-shock cognate 70 KDa protein was detected in three spots (1, 2, and 3), and this protein belongs to the heat-shock protein 70 family [56,57], along with heat-shock 70 KDa protein (spot 9). Hsp 70 and Hsc 70 are chaperones found in all organisms, from bacteria to humans, in the cell membrane, cytoplasm, nucleus, endoplasmic reticulum, and mitochondria, and play a critical role in various biological processes involving both systemic and cellular stress related to changes in temperature [58,59].…”

Comparative Transcripto me Analysis Depicts Candidate Genes Involved in Skin Color Differentiation in Red Tilapia

“…Heat shock protein (HSP70) is one of the most conservative and important proteins in HSPP family which is synthesized by the reaction of organism to the physical, chemical and biological stress agents in the environment [21]. HSP70 gene can produce abundant heat stress proteins, remove the denatured proteins, protect the cells from the damage of denatured proteins, and reduce the impact of external stress environment on the body of sh when the cells are under stress [22]. Studies have found that the HSP70 mRNA expression in the liver was signi cantly increased after 12 hrs of low-temperature stress on the sh [23].…”