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Genomics. 1991 Sep;11(1):206-11.

In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.

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Laboratory of Molecular Genetics, National Public Health Institute, Helsinki, Finland.


Aspartylglucosaminuria (AGU) is a lysosomal storage disease resulting in severe mental retardation. We have recently reported that mutations in the aspartylglucosaminidase (AGA) locus are responsible for this disease. About 90% of reported AGU cases are found in Finland, and we have shown that the vast majority (98%) of AGU alleles in this isolated population contain two point mutations located 5 bp apart. We expressed these Arg161----Gln and Cys163----Ser mutations separately in vitro and demonstrated that deficient enzyme activity is caused by the Cys163----Ser mutation, whereas the Arg161----Gln substitution represents a rare polymorphism. Further analyses of in vitro expressed AGA proteins and the enzyme purified from an AGU patient revealed that Cys163 participates in and S-S bridge. The absence of this covalent cross-link in the mutated protein most probably results in disturbed folding of the polypeptide chain and a consequent decrease in its intracellular stability.

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