Isolation and characterization of a cDNA encoding a Xenopus 70-kDa heat shock cognate protein, Hsc70.I.

We isolated a full-length cDNA clone encoding a Xenopus laevis 70-kDa heat shock cognate protein, hsc70.I. The protein coding region exhibits a high degree of identity with a number of mammalian hsc70 proteins, such as rat hsc71 (92%), whereas the identity to Xenopus hsp70 is only 80%. These data suggest that the inducible and constitutive forms of hsp70 diverged long before the emergence of amphibians. The Xenopus hsc70.I contains a number of conserved elements, including the ATP-binding domain, a nuclear localization signal and the carboxy-terminal EEVD motif, which has been implicated in several activities associated with chaperonin function. Northern blot analyses revealed that maternal hsc70.I mRNA is present in cleavage and early blastula stages of Xenopus development. After the onset of zygotic transcription at the midblastula stage, the levels of hsc70.I message increase through to the tadpole stages. Furthermore, in contrast to hsp70 mRNA, the relative levels of hsc70.I mRNA are not enhanced after heat shock in embryos and in the kidney epithelial cell line, A6. The levels of hsc70.I mRNA are high in adult spleen and testis, with moderate levels in eye, heart, liver and brain and comparatively low levels in hindlimb muscle.