Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing

T. Forné, E. Labourier, E. Antoine, F. Rossi, I. Gallouzi, G. Cathala, J. Tazi, C. Brunel

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

In the spliceosome, the pre-mRNA, U2 and U6 snRNAs fold into a catalytic structure exhibiting striking similarities with domain V and VI of group II introns. Building of this tripartite structure implies that an evolutionary conserved base pairing between U4 and U6 snRNAs should be disrupted to allow potentially U6 catalytic residue to interact with U2 snRNAs and the pre-mRNA. The steps leading to U4/U6 disruption have been recently discovered and have been shown to involve a modification of the 3' end of U6 snRNA and the hnRNP C protein.
Original languageEnglish (US)
Pages (from-to)436-442
Number of pages7
JournalBiochimie
Volume78
Issue number6
DOIs
StatePublished - Jan 1 1996
Externally publishedYes

Bibliographical note

Generated from Scopus record by KAUST IRTS on 2022-09-13

ASJC Scopus subject areas

  • Biochemistry

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