Abstract
A NUCLEOSIDE triphosphatase activity showing broad substrate specificity has been found in nuclear envelope isolated from rat and pig liver, Tetrahymena macronucleus, and cultured SV-3T3 fibroblasts using the method of Harris and Milne1, and has been extensively characterised in this laboratory. There is evidence that in purified nuclear envelopes there is only one enzyme which catalyses nucleoside triphosphate hydrolysis: the activities observed with different substrates and metal ions are not additive, and they show a single pH optimum, the value of which varies with the source of the envelopes2. This enzyme seems to be localised in the nuclear pore complexes3. Several reports4–13 have indicated that ATP markedly stimulates the release of mRNA from isolated nuclei, but no evidence has been presented to suggest that this stimulation necessarily requires hydrolysis of the ATP. In this paper, however, we present evidence that the nucleoside triphosphatase is an essential component of the mechanism of nucleocytoplasmic translocation of ribonucleoprotein.
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AGUTTER, P., MCARDLE, H. & MCCALDIN, B. Evidence for involvement of nuclear envelope nucleoside triphosphatase in nucleocytoplasmic translocation of ribonucleoprotein. Nature 263, 165–167 (1976). https://doi.org/10.1038/263165a0
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DOI: https://doi.org/10.1038/263165a0
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