Journalartikel

Jahr der Veröffentlichung: 1990

Seiten: 6223-6229

Zeitschrift: Nucleic Acids Research

Bandnummer: 18

Heftnummer: 21

ISSN: 0305-1048

eISSN: 1362-4962

DOI Link: https://doi.org/10.1093/nar/18.21.6223

Verlag: Oxford University Press

Abstract: 
U4 snRNA is phylogenetically highly conserved and organized in several domains. To determine the function of each of the domains of human U4 snRNA in the multi-step process of snRNP and spliceosome assembly, we used reconstitution procedures in combination with snRNA mutagenesis. The highly conserved 5' terminal domain of U4 snRNA consists of the stem I and stem II regions that have been proposed to base pair with U6 snRNA, and the 5' stem-loop structure. We found that each of these structural elements is essential for spliceosome assembly. However, only the stem II region is required for U4-U6 interaction, and none of these elements for Sm protein binding. In contrast, the 3' terminal domain of U4 snRNA containing the Sm binding site is dispensable for both U4-U6 interaction and spliceosome assembly. Our results support an organization of the U4 snRNP into multiple functional domains, each of which acts at distinct stages of snRNP and spliceosome assembly.

Harvard-Zitierstil: Wersig, C. and Bindereif, A. (1990) Conserved domains of human U4 snRNA required for snRNP and spliceosome assembly., Nucleic Acids Research, 18(21), pp. 6223-6229. https://doi.org/10.1093/nar/18.21.6223

APA-Zitierstil: Wersig, C., & Bindereif, A. (1990). Conserved domains of human U4 snRNA required for snRNP and spliceosome assembly.. Nucleic Acids Research. 18(21), 6223-6229. https://doi.org/10.1093/nar/18.21.6223