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Developmental expression of Hsp90, Hsp70 and HSF during morphogenesis in the vetigastropod Haliotis asinina

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Abstract

Heat shock proteins (Hsps) have dual functions, participating in both the stress response and a broad range of developmental processes. At physiological temperatures, it has been demonstrated in deuterostomes (vertebrates) and ecdysozoans (insects) that Hsps are expressed in tissues that are undergoing differentiation and morphogenesis. Here we investigate the developmental expression of Hsp70, Hsp90 and their regulatory transcription factor heat shock transcription factor (HSF) in the marine gastropod Haliotis asinina, a representative of the 3rd major lineage of bilaterian animals, the Lophotrochozoa. HasHsp70, HasHsp90 and HasHSF are maternally expressed in H. asinina and are progressively restricted to the micromere lineage during cleavage. During larval morphogenesis, they are expressed in unique and overlapping patterns in the prototroch, foot, and mantle. Hsp expression peaked in these tissues during periods of cell differentiation and morphogenesis, returning to lower levels after morphogenesis was complete. These patterns of Hsp and HSF expression in H. asinina are akin to those observed in ecdysozoans and deuterostomes, with Hsps being activated in cells and tissues undergoing morphogenesis.

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Acknowledgements

The authors thank two anonymous reviewers for their insightful comments. This research was supported from grants from the Australian Research Council to BMD.

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Correspondence to Bernard M. Degnan.

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Communicated by M. Martindale

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Fig. S1

HasHsp90 full-length cDNA sequence. The HasHsp90 nucleotide sequence is presented with the conceptual amino acid translation below. ATP interaction domain highlighted in light grey, charged linker underlined once, middle domain in dark grey and dimerisation domain is underlined twice. The stop codon is indicated by a full stop (DOC 32 kb)

Fig. S2

HasHsp70 partial sequence. cDNA fragment from the ATPase and protein interaction domain. The HasHsp70 nucleotide sequence is presented with the conceptual amino acid translation below. Highlighted areas represent conserved sequence motifs of heat inducible Hsp70 identified in Rensing and Maier (1994) and Kourtidis et al. (2006). The numbering is based purely on the fragment and does not relate to the 3′ end of the ORF (DOC 31 kb)

Fig. S3

HasHSF full-length sequence. The nucleotide sequence is presented with the conceptual amino acid translation below. The DNA binding domain is highlighted in light grey and the leucine zipper domains are underlined. The stop codon is indicated by a full stop (DOC 37 kb)

Table S1

Genbank accession numbers for sequences used in phylogenetic analyses (DOC 50 kb)

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Gunter, H.M., Degnan, B.M. Developmental expression of Hsp90, Hsp70 and HSF during morphogenesis in the vetigastropod Haliotis asinina . Dev Genes Evol 217, 603–612 (2007). https://doi.org/10.1007/s00427-007-0171-2

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