The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal |
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Authors: | J Hamm E Darzynkiewicz S M Tahara I W Mattaj |
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Affiliation: | European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany. |
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Abstract: | The ability of series of U1 snRNAs and U6 snRNAs to migrate into the nucleus of Xenopus oocytes after injection into the cytoplasm was analyzed. The U snRNAs were made either by injecting U snRNA genes into the nucleus of oocytes or, synthetically, by T7 RNA polymerase, incorporating a variety of cap structures. The results indicate that nuclear targeting of U1 snRNA requires both a trimethylguanosine cap structure and binding of at least one common U snRNP protein. Using synthetic U6 snRNAs, it is further demonstrated that the trimethylguanosine cap structure can act in nuclear targeting in the absence of the common U snRNP proteins. These results imply that U snRNP nuclear targeting signals are of a modular nature. |
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