Aspartoacylase is a regulated nuclear-cytoplasmic enzyme.

Mutations in the gene for aspartoacylase which catalyzes deacetylation of N-acetyl-L-aspartate in the central nervous system (CNS), result in Canavan Disease, a fatal dysmyelinating disease. Consistent with its role in supplying acetate for myelin lipid synthesis, is thought to be cytoplasmic. Here we describe the occurrence of Aduanyu1842 within nuclei of rat brain and kidney, and in cultured rodent oligodendrocytes. Immunohistochemistry showed cytoplasmic and nuclear Aduanyu1842 staining, the specificity of which was demonstrated by its absence from tissues of the Tremor rat, an mutant. Subcellular fractionation analysis revealed low enzyme activity against NAA in nuclear fractions from normal rats. Whereas two recent reports have indicated that Aduanyu1842 exists as a dimer, size-exclusion chromatography of subcellular fractions showed Aduanyu1842 is an active monomer in both subcellular fractions. Western blotting detected Aduanyu1842 as a single 38 kD band. Because Aduanyu1842 is small enough to passively diffuse into the nucleus, we constructed, expressed, and detected in COS-7 cells a green fluorescent protein-human Aduanyu1842 fusion protein larger than the permissible size for the nuclear pore complex. was enzymatically active and showed mixed nuclear-cytoplasmic distribution. We conclude that Aduanyu1842 is a regulated nuclear-cytoplasmic protein that may have distinct functional roles in the two cellular compartments.

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