MRNA-directed synthesis of catalytically active mouse beta-glucuronidase in Xenopus oocytes.

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Abstract
Catalytically active mouse .beta.-glucuronidase (.beta.-D-glucuronide glucuronosohydrolase, EC 3.2.1.31) is formed when X. laevis oocytes are injected with mouse RNA enriched for poly(A)-containing mRNA sequences. With the RNA from androgen-induced kidneys, the efficiency of translation is comparable to that of endogenous Xenopus messenger, and the fidelity of translation is high. Detection of glucuronidase messenger by formation of a catalytically active product is several orders of magnitude more sensitive than detection by incorporation of isotopically lableled amino acids. As well as providing a sensitive technique for examining the regulation of gene expression, the system makes available an opportunity to study the regulation of post-translational polypeptide processing of a lysosomal enzyme.