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Original Article

Molecular characterization of heat shock protein 90 from the dinoflagellate Prorocentrum donghaiense and its transcriptional response to thermal, copper and nutrient stresses

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Pages 343-356 | Received 16 Nov 2018, Accepted 21 May 2019, Published online: 05 Sep 2019
 

ABSTRACT

In this study, a novel HSP90 gene (PdHSP90) was cloned from Prorocentrum donghaiense. The full length of PdHSP90 is 2443 bp, with 5′-UTR of 111 bp, 3′-UTR of 199 bp, and open reading frame (ORF) of 2133 bp. The ORF encodes a polypeptide of 710 amino acid residues, with molecular weight of approximately 85.81 kDa and isoelectric point of 4.95. Phylogenetic analysis revealed that PdHSP90 belongs to the dinoflagellate clade and is closely related to HSP90s from P. minimum and P. micans. PdHSP90 expression increased under the thermal stress (p < 0.05), with the highest changes of 7.6-fold at 10°C 2 h post treatment compared to the control. PdHSP90 expression was significantly upregulated (1- to 10.8-fold change) (p < 0.05) with increasing concentrations of copper from 0 µM to 31.25 µM. PdHSP90 expression level under 176 µM nitrogen was nearly equal to that under 88 µM nitrogen, which were 4.5- and 4.6-fold higher, respectively, compared with the control (p < 0.05). Upon treatment with phosphorus limitation from 36 µM to 3.6 µM, PdHSP90 transcription level increased 11.4-fold (p < 0.05) and then decreased. These results provide new insights into the molecular mechanism underlying adaptation of P. donghaiense and other harmful dinoflagellates in response to diverse environmental factors.

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Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

This work was supported by the National Scientific Foundation of China (No. 31600309, 41476086, 41106082); HIT Scientific Research Innovation Fund/the Fundamental Research Funds for the Central Universities (No. HIT.NSRIF.201702 and HIT.NSRIF.201709); and the K.C.Wong Magna Fund in Ningbo University.

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