Journal article

Publication year: 1990

Pages: 6223-6229

Journal: Nucleic Acids Research

Volume number: 18

Issue number: 21

ISSN: 0305-1048

eISSN: 1362-4962

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

Publisher: 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 Citation style: 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 Citation style: 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