Spermatogenesis in the archaic hydrothermal vent bivalve,Bathypecten vulcani,and comparison of spermatozoon ultrastructure with littoral pectinids

Summary

Bathypecten vulcani is considered a relict species from the Paleozoic, based on shell characteristics such as the presence of calcite prisms. To date, it is the only pectinid species reported from hydrothermal ecosystems. Histological and ultrastructural studies show that spermatogenesis is identical to that of littoral pectinids. The spermatozoon has a 2.7 μm long pyriform head and a 40 μm flagellum. The four mitochondria of the mid-piece are about 1.2 μm in diameter. The nucleus contains dense chromatin fibres and possesses a wide, shallow (0.1 μm) anterior fossa and a narrow, deeper (0.2 μm) posterior nuclear fossa. Comparison of the ultrastructural characteristics of the spermatozoon of B. vulcani with those of littoral pectinids shows that they can be used as a diagnostic feature of this species. In particular, its acrosome characters will be a useful complement to the shell characters in the study of the phylogenetic position of this species in relation to other pectinids.     

Stch encodes the 'ATPase core' of a microsomal stress 70 protein.

The stress70 protein chaperone family plays a central role in the processing of cytosolic and secretory proteins. We have cloned a human cDNA, designated Stch, that is conserved in rat tissues and which encodes a novel microsome-associated member of the stress70 protein chaperone family. Stch mRNA is constitutively expressed in all human cell types and is induced by incubation with the calcium ionophore A23187, but not by exposure to heat shock. Inspection of the predicted amino acid sequence reveals that the STCH product contains a unique hydrophobic leader sequence and shares homology within the amino terminal domains of the stress70 gene family, but has a 50 residue insertion within the ATP-binding domains and truncates the carboxyl terminal peptide-binding region. Immunofluorescent and subcellular analyses show that STCH migrates predominantly as a 60 kDa species and is enriched in a membrane-bound microsome fraction. In contrast to purified BiP and dnaK, however, STCH demonstrates ATPase activity that is independent of peptide stimulation. Stch, therefore, encodes a calcium-inducible, microsome-associated ATPase activity with properties similar to a proteolytically cleaved N-terminal HSC70/BiP fragment. This truncated stress70 molecule may allow increased diversity in cellular responses to protein processing requirements.