Journalartikel

Jahr der Veröffentlichung: 1992

Seiten: 1460-1468

Zeitschrift: Molecular and Cellular Biology

Bandnummer: 12

Heftnummer: 4

ISSN: 0270-7306

eISSN: 1098-5549

DOI Link: https://doi.org/10.1128/MCB.12.4.1460

Verlag: Taylor and Francis Group

Abstract: 
We have developed an in vitro splicing complementation assay to investigate the domain structure of the mammalian U4 small nuclear RNA (snRNA) through mutational analysis. The addition of affinity-purified U4 snRNP or U4 RNA to U4-depleted nuclear extract efficiently restores splicing activity. In the U4-U6 interaction domain of U4 RNA, only stem II was found to be essential for splicing activity; the 5' loop is important for spliceosome stability. In the central domain, we have identified a U4 RNA sequence element that is important for splicing and spliceosome assembly. Surprisingly, an intact Sm domain is not essential for splicing in vitro. Our data provide evidence that several distinct regions of U4 RNA contribute to snRNP assembly, spliceosome assembly and stability, and splicing activity.

Harvard-Zitierstil: Wersig, C. and Bindereif, A. (1992) Reconstitution of functional mammalian U4 small nuclear ribonucleoprotein: Sm protein binding is not essential for splicing in vitro., Molecular and Cellular Biology, 12(4), pp. 1460-1468. https://doi.org/10.1128/MCB.12.4.1460

APA-Zitierstil: Wersig, C., & Bindereif, A. (1992). Reconstitution of functional mammalian U4 small nuclear ribonucleoprotein: Sm protein binding is not essential for splicing in vitro.. Molecular and Cellular Biology. 12(4), 1460-1468. https://doi.org/10.1128/MCB.12.4.1460