Molecular cloning of rat ATX1 homologue protein.

Abstract

An ATX1 homologue of 503 bp length was cloned from a rat cDNA library, and the deduced protein from the cDNA was found to contain 68 amino acids with a predicted molecular mass of 7.2 kDa. The rat ATX1 homologue protein (Rah1p), which shows 35%, 38%, and 89% identities with Atx1p, CUC-1, and HAH1, respectively, conserves both the MTCXXC copper-binding site in the N terminus and the KTGK lysine-rich region in the C terminus. In Northern blot analysis, rah1 mRNA was found to be expressed at high levels in the liver, small intestine, and testis. Expression of rah1 cDNA complemented a null atx1 mutant strain in yeast. Thus, Rah1p was concluded to be a functional copper chaperone.

Cite this paper

@article{Hiromura1999MolecularCO, title={Molecular cloning of rat ATX1 homologue protein.}, author={Makoto Hiromura and Hiroaki Sakurai}, journal={Biochemical and biophysical research communications}, year={1999}, volume={265 2}, pages={509-12} }