scholarly journals The U1 RNA-Binding Site of the U1 Small Nuclear Ribonucleoprotein (snRNP)-Associated A Protein Suggests a Similarity with U2 snRNPs:

1989 ◽  
Vol 9 (10) ◽  
pp. 4585-4585
Keyword(s):  
Binding Site ◽  
Rna Binding ◽  
Small Nuclear Ribonucleoprotein ◽  
Nuclear Ribonucleoprotein

scholarly journals The small nuclear ribonucleoprotein SS-B/La binds RNA with a conserved protease-resistant domain of 28 kilodaltons.

1987 ◽  
Vol 7 (7) ◽  
pp. 2588-2591 ◽  
Author(s):  
E K Chan ◽  
E M Tan
Keyword(s):  
Binding Site ◽  
Gel Electrophoresis ◽  
Nuclear Protein ◽  
Rna Binding ◽  
Cross Link ◽  
Structural Domains ◽  
Small Nuclear Ribonucleoprotein ◽  
Protease Digestion ◽  
Nuclear Ribonucleoprotein ◽  
Rna Complexes

SS-B/La is a nuclear protein of 48 kilodaltons with two structural domains of Mr 28,000 and Mr 23,000 generated by proteolytic cleavage. UV irradiation was used to cross-link preexisting intracellular La-RNA complexes. Subsequent protease digestion and diagonal gel electrophoresis showed that the RNA-binding site resided in the nonphosphorylated, methionine-rich 28-kilodalton domain.

scholarly journals The U1 RNA-binding site of the U1 small nuclear ribonucleoprotein (snRNP)-associated A protein suggests a similarity with U2 snRNPs.

1989 ◽  
Vol 9 (7) ◽  
pp. 2975-2982 ◽  
Author(s):  
C Lutz-Freyermuth ◽  
J D Keene ◽  
C Lutz-Reyermuth
Keyword(s):  
Binding Site ◽  
Rna Binding ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Stem Loop ◽  
Small Nuclear Ribonucleoprotein ◽  
Vitro Binding ◽  
Associated Proteins ◽  
Nuclear Ribonucleoprotein

The site of interaction between human U1 RNA and one of its uniquely associated proteins, A, was examined with in vitro binding assays. The A protein bound directly to stem-loop II of U1 RNA in a region which exhibits sequence similarity to U2 RNA. The similarity with U2 RNA was in a region that has been shown to interact with a U2 RNA-associated protein. The A protein-binding site on U1 RNA overlapped a previously described epitope for an RNA-specific human autoantibody (S. L. Deutscher and J. D. Keene, Proc. Natl. Acad. Sci. USA 85:3299-3303, 1988), supporting the hypothesis that the anti-RNA antibody originated as an anti-idiotypic response to A protein-specific autoantibodies.

The small nuclear ribonucleoprotein SS-B/La binds RNA with a conserved protease-resistant domain of 28 kilodaltons

1987 ◽  
Vol 7 (7) ◽  
pp. 2588-2591
Author(s):  
E K Chan ◽  
E M Tan
Keyword(s):  
Binding Site ◽  
Gel Electrophoresis ◽  
Nuclear Protein ◽  
Rna Binding ◽  
Cross Link ◽  
Structural Domains ◽  
Small Nuclear Ribonucleoprotein ◽  
Protease Digestion ◽  
Nuclear Ribonucleoprotein ◽  
Rna Complexes

SS-B/La is a nuclear protein of 48 kilodaltons with two structural domains of Mr 28,000 and Mr 23,000 generated by proteolytic cleavage. UV irradiation was used to cross-link preexisting intracellular La-RNA complexes. Subsequent protease digestion and diagonal gel electrophoresis showed that the RNA-binding site resided in the nonphosphorylated, methionine-rich 28-kilodalton domain.

scholarly journals Identification and characterization of a yeast gene encoding the U2 small nuclear ribonucleoprotein particle B" protein.

1996 ◽  
Vol 16 (6) ◽  
pp. 2787-2795 ◽  
Author(s):  
J Tang ◽  
N Abovich ◽  
M Rosbash
Keyword(s):  
Binding Site ◽  
Rna Binding ◽  
Yeast Gene ◽  
Ribonucleoprotein Particle ◽  
Synthetic Lethal ◽  
U2 Snrna ◽  
Small Nuclear Ribonucleoprotein ◽  
Nuclear Ribonucleoprotein ◽  
U1a Protein ◽  
Small Nuclear Ribonucleoprotein Particle

The inessential yeast gene MUD2 encodes a protein factor that contributes to U1 small nuclear ribonucleoprotein particle (snRNP)-pre-mRNA complex (commitment complex) formation. To identify other genes that contribute to this early splicing step, we performed a synthetic lethal screen with a MUD2 deletion strain. The first characterized gene from this screen, MSL1 (MUD synthetic lethal 1), encodes the yeast homolog of the well studied mammalian snRNP protein U2B". The yeast protein (YU2B") is a component of yeast U2 snRNP, and it is related to other members of the UIA-U2B" family, the human U2B" protein, the human U1A protein, and the yeast U1A protein. It binds in vitro to its RNA target, U2 snRNA stem-loop IV, without a protein cofactor, and the target resembles more closely the U1 snRNA binding site of the human U1A protein than it does the U2 snRNA binding site of human U2B". Surprisingly, the YU2B" protein lacks a C-terminal RNA binding domain, which is conserved in all other family members. Possible functional and evolutionary relationships among these proteins are discussed.

The U1 RNA-binding site of the U1 small nuclear ribonucleoprotein (snRNP)-associated A protein suggests a similarity with U2 snRNPs

1989 ◽  
Vol 9 (7) ◽  
pp. 2975-2982
Author(s):  
C Lutz-Freyermuth ◽  
J D Keene ◽  
C Lutz-Reyermuth
Keyword(s):  
Binding Site ◽  
Rna Binding ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Stem Loop ◽  
Small Nuclear Ribonucleoprotein ◽  
Vitro Binding ◽  
Associated Proteins ◽  
Nuclear Ribonucleoprotein

The site of interaction between human U1 RNA and one of its uniquely associated proteins, A, was examined with in vitro binding assays. The A protein bound directly to stem-loop II of U1 RNA in a region which exhibits sequence similarity to U2 RNA. The similarity with U2 RNA was in a region that has been shown to interact with a U2 RNA-associated protein. The A protein-binding site on U1 RNA overlapped a previously described epitope for an RNA-specific human autoantibody (S. L. Deutscher and J. D. Keene, Proc. Natl. Acad. Sci. USA 85:3299-3303, 1988), supporting the hypothesis that the anti-RNA antibody originated as an anti-idiotypic response to A protein-specific autoantibodies.

scholarly journals The U1 small nuclear ribonucleoprotein (snRNP) 70K protein is transported independently of U1 snRNP particles via a nuclear localization signal in the RNA-binding domain.

1994 ◽  
Vol 14 (7) ◽  
pp. 4662-4670 ◽  
Author(s):  
J M Romac ◽  
D H Graff ◽  
J D Keene
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Rna Binding ◽  
Binding Domain ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Small Nuclear Ribonucleoprotein ◽  
Localization Signal ◽  
Nuclear Ribonucleoprotein

Expression of the recombinant human U1-70K protein in COS cells resulted in its rapid transport to the nucleus, even when binding to U1 RNA was debilitated. Deletion analysis of the U1-70K protein revealed the existence of two segments of the protein which were independently capable of nuclear localization. One nuclear localization signal (NLS) was mapped within the U1 RNA-binding domain and consists of two typically separated but interdependent elements. The major element of this NLS resides in structural loop 5 between the beta 4 strand and the alpha 2 helix of the folded RNA recognition motif. The C-terminal half of the U1-70K protein which was capable of nuclear entry contains two arginine-rich regions, which suggests the existence of a second NLS. Site-directed mutagenesis of the RNA recognition motif NLS demonstrated that the U1-70K protein can be transported independently of U1 RNA and that its association with the U1 small nuclear ribonucleoprotein particle can occur in the nucleus.

Molecular cloning of Xenopus fibrillarin, a conserved U3 small nuclear ribonucleoprotein recognized by antisera from humans with autoimmune disease

1990 ◽  
Vol 10 (1) ◽  
pp. 430-434 ◽  
Author(s):  
B Lapeyre ◽  
P Mariottini ◽  
C Mathieu ◽  
P Ferrer ◽  
F Amaldi ◽  
...  
Keyword(s):  
Autoimmune Disease ◽  
Xenopus Laevis ◽  
Cdna Library ◽  
Protein Sequence ◽  
Rna Binding ◽  
Consensus Sequence ◽  
Ribonucleoprotein Particle ◽  
Rich Domain ◽  
Small Nuclear Ribonucleoprotein ◽  
Nuclear Ribonucleoprotein

Autoantibodies against U3 small nuclear ribonucleoprotein are associated with scleroderma autoimmune disease. They were shown to react with fibrillarin, a 34- to 36-kilodalton protein that has been detected in all eukaryotes tested from humans to yeasts. We isolated a 1.6-kilobase cDNA encoding fibrillarin from a Xenopus laevis cDNA library. The protein contains a 79-residue-long Gly-Arg-rich domain in its N-terminal region and a putative RNA-binding domain with ribonucleoprotein consensus sequence in its central portion. This is the first report of cloning of fibrillarin, and the deduced protein sequence is in agreement with the involvement of the protein in a ribonucleoprotein particle.

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