Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing.
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.
Institut de Génétique Moléculaire, UMR 5535, CNRS, Université de Montpellier II, France.
T
T
Forné
E
E
Labourier
E
E
Antoine
F
F
Rossi
I
I
Gallouzi
G
G
Cathala
J
J
Tazi
C
C
Brunel
D001482:Base Composition; D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D009690:Nucleic Acid Conformation; D012322:RNA Precursors / Q000378:metabolism*; D012326:RNA Splicing / Q000235:genetics*; D012342:RNA, Small Nuclear / Q000737:chemistry* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism; D017381:Spliceosomes / Q000378:metabolism*
D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D012322:RNA Precursors; D012342:RNA, Small Nuclear; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins