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Nucleic Acids Research, 1983, Vol. 11, No. 19 6631-6646
© 1983

MOLECULAR BIOLOGY

Interaction of snRNAs with rapidly sedimenting nuclear sub-structures (hnRNPs) from HeLa cells

Joannès Sri-Widada, Jean-Pierre Liautard, Claude Brunel and Philippe Jeanteur

Laboratoire de Biochimie, Centre Paul Lamarque BP 5053, 34033 Montpellier and Laboratoire de Biologie Moléculaire, Université des Sciences et Techniques du Languedoc 34060, Montpellier, France

Received August 1, 1983. Accepted September 8, 1983.

We have shown previously (Liautard et al., 1982, J. Mol. Biol., 162, 623–643) that digestion with micrococcal nuclease under drastic conditions of a pure U1 snRNP, as well as a mixture containing U2, U1, U4, U5 and U6 snRNPs, gives rise to resistant RNA fragments derived from all but U6 snRNAs. As an attempt to elucidate the way in which snRNPs are attached to their native structure, the same approach was applied to hnRNP which are known to contain snRNP (Guimont-Ducamp et al., 1977, Biochimie, 59, 755–758). Micrococcal nuclease digestion of hnRNPs yielded a population of 15–50 nucleotides long resistant fragments of snRNAs. Sequence analyses showed that all fragments previously identified in core snRNPs were also present. Only U2 and U5 snRNAs were further protected as a result of their association with the hnRNP complex (from the cap to nucleotide 32 for U2 and from nucleotide 22 to nucleotide 70 for U5). No additional protected fragment derived from U1, U4 and U6 snRNAs was found. This finding confirms that the 5' terminal region of U1 snRNP remains available for base-pairing interaction with the premessenger RNA, as predicted by the model of Lerner et al. (Nature, 1980, 283, 220–224).


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