scholarly journals RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.

1991 ◽  
Vol 88 (6) ◽  
pp. 2495-2499 ◽  
Author(s):  
D. W. Hoffman ◽  
C. C. Query ◽  
B. L. Golden ◽  
S. W. White ◽  
J. D. Keene
Keyword(s):  
Nmr Spectroscopy ◽  
Ribosomal Proteins ◽  
Rna Binding ◽  
Binding Domain ◽  
Protein Component ◽  
Small Nuclear Ribonucleoprotein ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A

Nature ◽  
1990 ◽  
Vol 348 (6301) ◽  
pp. 515-520 ◽  
Author(s):  
Kiyoshi Nagai ◽  
Chris Oubridge ◽  
Timm H. Jessen ◽  
Jade Li ◽  
Philip R. Evans
Keyword(s):  
Crystal Structure ◽  
Rna Binding ◽  
Binding Domain ◽  
Small Nuclear Ribonucleoprotein ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

scholarly journals T Cell Immunity in Connective Tissue Disease Patients Targets the RNA Binding Domain of the U1-70kDa Small Nuclear Ribonucleoprotein

2002 ◽  
Vol 169 (6) ◽  
pp. 3429-3437 ◽  
Author(s):  
Eric L. Greidinger ◽  
Mark F. Foecking ◽  
Kim R. Schäfermeyer ◽  
Craig W. Bailey ◽  
Shannon L. Primm ◽  
...  
Keyword(s):  
T Cell ◽  
Connective Tissue ◽  
Connective Tissue Disease ◽  
Rna Binding ◽  
Binding Domain ◽  
T Cell Immunity ◽  
Small Nuclear Ribonucleoprotein ◽  
Cell Immunity ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

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.

scholarly journals A specific 31-nucleotide domain of U1 RNA directly interacts with the 70K small nuclear ribonucleoprotein component.

1989 ◽  
Vol 9 (11) ◽  
pp. 4872-4881 ◽  
Author(s):  
C C Query ◽  
R C Bentley ◽  
J D Keene
Keyword(s):  
Nucleotide Sequence ◽  
Splice Site ◽  
Rna Binding ◽  
Binding Domain ◽  
Specific Domain ◽  
Stem Loop ◽  
Small Nuclear Ribonucleoprotein ◽  
Associated Proteins ◽  
Nuclear Ribonucleoprotein

We have defined the nucleotide sequence of a protein-binding domain within U1 RNA that specifically recognizes and binds both to a U1 small nuclear ribonucleoprotein component (the 70K protein) and to the previously defined RNA-binding domain of the 70K protein. We have investigated direct interactions between purified U1 RNA and 70K protein by reconstitution in vitro. Thirty-one nucleotides of U1 RNA, corresponding to stem-loop I, were required for this interaction. Nucleotides at the 5' end of U1 RNA that are involved in base pairing with the 5' splice site of pre-mRNA were not required for binding. In contrast to other reports, these findings demonstrate that a specific domain of U1 RNA can bind directly to the 70K protein independently of any other snRNP-associated proteins.

scholarly journals Insight into Mammalian Selenocysteine Insertion: Domain Structure and Ribosome Binding Properties of Sec Insertion Sequence Binding Protein 2

2001 ◽  
Vol 21 (5) ◽  
pp. 1491-1498 ◽  
Author(s):  
Paul R. Copeland ◽  
Vincent A. Stepanik ◽  
Donna M. Driscoll
Keyword(s):  
Ribosomal Proteins ◽  
Insertion Sequence ◽  
Rna Binding ◽  
Stop Codon ◽  
Binding Protein ◽  
Binding Domain ◽  
Site Directed Mutagenesis ◽  
Functional Domain ◽  
28S Rrna ◽  
Rna Binding Domain

ABSTRACT The cotranslational incorporation of the unusual amino acid selenocysteine (Sec) into both prokaryotic and eukaryotic proteins requires the recoding of a UGA stop codon as one specific for Sec. The recognition of UGA as Sec in mammalian selenoproteins requires a Sec insertion sequence (SECIS) element in the 3′ untranslated region as well as the SECIS binding protein SBP2. Here we report a detailed analysis of SBP2 structure and function using truncation and site-directed mutagenesis. We have localized the RNA binding domain to a conserved region shared with several ribosomal proteins and eukaryotic translation termination release factor 1. We also identified a separate and novel functional domain N-terminal to the RNA binding domain which was required for Sec insertion but not for SECIS binding. Conversely, we showed that the RNA binding domain was necessary but not sufficient for Sec insertion and that the conserved glycine residue within this domain was required for SECIS binding. Using glycerol gradient sedimentation, we found that SBP2 was stably associated with the ribosomal fraction of cell lysates and that this interaction was not dependent on its SECIS binding activity. This interaction also occurred with purified components in vitro, and we present data which suggest that the SBP2-ribosome interaction occurs via 28S rRNA. SBP2 may, therefore, have a distinct function in selecting the ribosomes to be used for Sec insertion.

A specific 31-nucleotide domain of U1 RNA directly interacts with the 70K small nuclear ribonucleoprotein component

1989 ◽  
Vol 9 (11) ◽  
pp. 4872-4881
Author(s):  
C C Query ◽  
R C Bentley ◽  
J D Keene
Keyword(s):  
Nucleotide Sequence ◽  
Splice Site ◽  
Rna Binding ◽  
Binding Domain ◽  
Specific Domain ◽  
Stem Loop ◽  
Small Nuclear Ribonucleoprotein ◽  
Associated Proteins ◽  
Nuclear Ribonucleoprotein

We have defined the nucleotide sequence of a protein-binding domain within U1 RNA that specifically recognizes and binds both to a U1 small nuclear ribonucleoprotein component (the 70K protein) and to the previously defined RNA-binding domain of the 70K protein. We have investigated direct interactions between purified U1 RNA and 70K protein by reconstitution in vitro. Thirty-one nucleotides of U1 RNA, corresponding to stem-loop I, were required for this interaction. Nucleotides at the 5' end of U1 RNA that are involved in base pairing with the 5' splice site of pre-mRNA were not required for binding. In contrast to other reports, these findings demonstrate that a specific domain of U1 RNA can bind directly to the 70K protein independently of any other snRNP-associated proteins.

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.

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