Nuclear transport of proteins translated in vitro from SP6 plasmid-generated mRNAs.
Open Access
- 1 March 1990
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 10 (3) , 1287-1292
- https://doi.org/10.1128/mcb.10.3.1287
Abstract
A sensitive and versatile assay is described for the nuclear transport of 35S-labeled proteins obtained by the in vitro translation of SP6 plasmid-generated mRNAs. A specific nuclear accumulation of greater than 20-fold is observed for the transformation-related nuclear proteins, p53 and E1b, and the nuclear enzyme, thymidine kinase, whereas transport of the nonnuclear proteins, dihydrofolate reductase and simian virus 40 small t antigen, is negligible within 30 min.This publication has 38 references indexed in Scilit:
- Identification of specific binding proteins for a nuclear location sequenceNature, 1989
- Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocationCell, 1988
- Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobilityBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1986
- In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins.The Journal of cell biology, 1986
- Uncoupling Translocation from Translation: Implications for Transport of Proteins Across MembranesScience, 1986
- Nuclear location signals in polyoma virus large-TCell, 1985
- A large particle associated with the perimeter of the nuclear pore complex.The Journal of cell biology, 1982
- Structure and genomic organization of the mouse dihydrofolate reductase geneCell, 1980
- ON THE ATTACHMENT OF THE NUCLEAR PORE COMPLEXThe Journal of cell biology, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970