scholarly journals Architectural Arrangement of the Small Nuclear RNA (snRNA)-activating Protein Complex 190 Subunit (SNAP190) on U1 snRNA Gene Promoter DNA

2012 ◽  
Vol 287 (47) ◽  
pp. 39369-39379 ◽  
Author(s):  
Matthew T. Doherty ◽  
Yoon Soon Kang ◽  
Cheryn Lee ◽  
William E. Stumph
Keyword(s):  
Protein Complex ◽  
Gene Promoter ◽  
Small Nuclear Rna ◽  
Snrna Gene ◽  
U1 Snrna ◽  
Nuclear Rna ◽  
Promoter Dna

An mRNA-type intron is present in the Rhodotorula hasegawae U2 small nuclear RNA gene

1993 ◽  
Vol 13 (9) ◽  
pp. 5613-5619
Author(s):  
Y Takahashi ◽  
S Urushiyama ◽  
T Tani ◽  
Y Ohshima
Keyword(s):  
Mrna Splicing ◽  
Small Nuclear Rna ◽  
U2 Snrna ◽  
U6 Snrna ◽  
Branch Site ◽  
Snrna Gene ◽  
Nuclear Rna ◽  
Catalytic Role ◽  
Mrna Precursor ◽  
Site Recognition

Splicing an mRNA precursor requires multiple factors involving five small nuclear RNA (snRNA) species called U1, U2, U4, U5, and U6. The presence of mRNA-type introns in the U6 snRNA genes of some yeasts led to the hypothesis that U6 snRNA may play a catalytic role in pre-mRNA splicing and that the U6 introns occurred through reverse splicing of an intron from an mRNA precursor into a catalytic site of U6 snRNA. We characterized the U2 snRNA gene of the yeast Rhodotorula hasegawae, which has four mRNA-type introns in the U6 snRNA gene, and found an mRNA-type intron of 60 bp. The intron of the U2 snRNA gene is present in the highly conserved region immediately downstream of the branch site recognition domain. Interestingly, we found that this region can form a novel base pairing with U6 snRNA. We discuss the possible implications of these findings for the mechanisms of intron acquisition and for the role of U2 snRNA in pre-mRNA splicing.

Crystal structure of the spliceosomal U2B″–U2A′ protein complex bound to a fragment of U2 small nuclear RNA

Nature ◽  
10.1038/29234 ◽  
1998 ◽  
Vol 394 (6694) ◽  
pp. 645-650 ◽  
Author(s):  
Stephen R. Price ◽  
Philip R. Evans ◽  
Kiyoshi Nagai
Keyword(s):  
Crystal Structure ◽  
Protein Complex ◽  
Small Nuclear Rna ◽  
Nuclear Rna

The U1 small nuclear RNA-protein complex selectively binds a 5′ splice site in vitro

Cell ◽  
1983 ◽  
Vol 33 (2) ◽  
pp. 509-518 ◽  
Author(s):  
Stephen M. Mount ◽  
Ingvar Pettersson ◽  
Monique Hinterberger ◽  
Aavo Karmas ◽  
Joan A. Steitz
Keyword(s):  
Splice Site ◽  
Protein Complex ◽  
Small Nuclear Rna ◽  
Nuclear Rna

scholarly journals An mRNA-type intron is present in the Rhodotorula hasegawae U2 small nuclear RNA gene.

1993 ◽  
Vol 13 (9) ◽  
pp. 5613-5619 ◽  
Author(s):  
Y Takahashi ◽  
S Urushiyama ◽  
T Tani ◽  
Y Ohshima
Keyword(s):  
Mrna Splicing ◽  
Small Nuclear Rna ◽  
U2 Snrna ◽  
U6 Snrna ◽  
Branch Site ◽  
Snrna Gene ◽  
Nuclear Rna ◽  
Catalytic Role ◽  
Mrna Precursor ◽  
Site Recognition

Splicing an mRNA precursor requires multiple factors involving five small nuclear RNA (snRNA) species called U1, U2, U4, U5, and U6. The presence of mRNA-type introns in the U6 snRNA genes of some yeasts led to the hypothesis that U6 snRNA may play a catalytic role in pre-mRNA splicing and that the U6 introns occurred through reverse splicing of an intron from an mRNA precursor into a catalytic site of U6 snRNA. We characterized the U2 snRNA gene of the yeast Rhodotorula hasegawae, which has four mRNA-type introns in the U6 snRNA gene, and found an mRNA-type intron of 60 bp. The intron of the U2 snRNA gene is present in the highly conserved region immediately downstream of the branch site recognition domain. Interestingly, we found that this region can form a novel base pairing with U6 snRNA. We discuss the possible implications of these findings for the mechanisms of intron acquisition and for the role of U2 snRNA in pre-mRNA splicing.

scholarly journals Direct, sequence-specific binding of the human U1-70K ribonucleoprotein antigen protein to loop I of U1 small nuclear RNA.

1989 ◽  
Vol 9 (10) ◽  
pp. 4179-4186 ◽  
Author(s):  
C S Surowy ◽  
V L van Santen ◽  
S M Scheib-Wixted ◽  
R A Spritz
Keyword(s):  
Fusion Protein ◽  
Rna Binding ◽  
Specific Binding ◽  
Consensus Sequence ◽  
Small Nuclear Rna ◽  
Small Nuclear Ribonucleoprotein ◽  
U1 Snrna ◽  
Nuclear Rna ◽  
Mutation Analyses

We have studied the interaction of two of the U1 small nuclear ribonucleoprotein (snRNP)-specific proteins, U1-70K and U1-A, with U1 small nuclear RNA (snRNA). The U1-70K protein is a U1-specific RNA-binding protein. Deletion and mutation analyses of a beta-galactosidase/U1-70K partial fusion protein indicated that the central portion of the protein, including the RNP sequence domain, is both necessary and sufficient for specific U1 snRNA binding in vitro. The highly conserved eight-amino-acid RNP consensus sequence was found to be essential for binding. Deletion and mutation analyses of U1 snRNA showed that both the U1-70K fusion protein and the native HeLa U1-70K protein bound directly to loop I of U1 snRNA. Binding was sequence specific, requiring 8 of the 10 bases in the loop. The U1-A snRNP protein also interacted specifically with U1 snRNA, principally with stem-loop II.

scholarly journals The Pre-mRNA 5′ Cap Determines Whether U6 Small Nuclear RNA Succeeds U1 Small Nuclear Ribonucleoprotein Particle at 5′ Splice Sites

1998 ◽  
Vol 18 (12) ◽  
pp. 7510-7520 ◽  
Author(s):  
Laura O’Mullane ◽  
Ian C. Eperon
Keyword(s):  
Splice Site ◽  
Major Effect ◽  
Small Nuclear Rna ◽  
Splice Sites ◽  
U6 Snrna ◽  
Small Nuclear Ribonucleoprotein ◽  
U1 Snrna ◽  
U1 Snrnp ◽  
Nuclear Rna ◽  
Nuclear Ribonucleoprotein

ABSTRACT Efficient splicing of the 5′-most intron of pre-mRNA requires a 5′ m7G(5′)ppp(5′)N cap, which has been implicated in U1 snRNP binding to 5′ splice sites. We demonstrate that the cap alters the kinetic profile of U1 snRNP binding, but its major effect is on U6 snRNA binding. With two alternative wild-type splice sites in an adenovirus pre-mRNA, the cap selectively alters U1 snRNA binding at the site to which cap-independent U1 snRNP binding is stronger and that is used predominantly in splicing; with two consensus sites, the cap acts on both, even though one is substantially preferred for splicing. However, the most striking quantitative effect of the 5′ cap is neither on U1 snRNP binding nor on the assembly of large complexes but on the replacement of U1 snRNP by U6 snRNA at the 5′ splice site. Inhibition of splicing by a cap analogue is correlated with the loss of U6 interactions at the 5′ splice site and not with any loss of U1 snRNP binding.

Sign in / Sign up

Export Citation Format

Share Document