scholarly journals The RNA binding site of bacteriophage MS2 coat protein.

1993 ◽  
Vol 12 (2) ◽  
pp. 595-600 ◽  
Author(s):  
D.S. Peabody
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
Rna Binding ◽  
Bacteriophage Ms2

scholarly journals Complementation of RNA Binding Site Mutations in MS2 Coat Protein Heterodimers

1996 ◽  
Vol 24 (12) ◽  
pp. 2352-2359 ◽  
Author(s):  
D. S. Peabody ◽  
F. Lim
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
Rna Binding

RNA binding site of R17 coat protein

Biochemistry ◽  
1987 ◽  
Vol 26 (6) ◽  
pp. 1563-1568 ◽  
Author(s):  
Paul J. Romaniuk ◽  
Peggy Lowary ◽  
Huey Nan Wu ◽  
Gary Stormo ◽  
Olke C. Uhlenbeck
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
Rna Binding

Interaction of R17 Coat Protein With Its RNA Binding Site For Translational Repression

1983 ◽  
Vol 1 (2) ◽  
pp. 539-552 ◽  
Author(s):  
Olke C. Uhlenbeck ◽  
Jannette Carey ◽  
Paul J. Romaniuk ◽  
Peggy T. Lowary ◽  
Dorothy Beckett
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
Rna Binding ◽  
Translational Repression

scholarly journals Combined Use of MS2 and PP7 Coat Fusions Shows that TIA-1 Dominates hnRNP A1 for K-SAM Exon Splicing Control

2009 ◽  
Vol 2009 ◽  
pp. 1-6 ◽  
Author(s):  
Marie-Claude Gesnel ◽  
Fabienne Del Gatto-Konczak ◽  
Richard Breathnach
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
The Other ◽  
Coat Proteins ◽  
Hnrnp A1 ◽  
Bacteriophage Ms2 ◽  
Exon Splicing ◽  
Mrna Molecule ◽  
Combined Use

Splicing of the FGFR2 K-SAM exon is repressed by hnRNP A1 bound to the exon and activated by TIA-1 bound to the downstream intron. Both proteins are expressed similarly by cells whether they splice the exon or not, so it is important to know which one is dominant. To answer this question, we used bacteriophage PP7 and bacteriophage MS2 coat fusions to tether hnRNP A1 and TIA-1 to distinct sites on the same pre-mRNA molecule. hnRNP A1 fused to one coat protein was tethered to a K-SAM exon containing the corresponding coat protein's binding site. TIA-1 fused to the other coat protein was tethered to the downstream intron containing that coat protein's binding site. This led to efficient K-SAM exon splicing. Our results show that TIA-1 is dominant for K-SAM exon splicing control and validate the combined use of PP7 and MS2 coat proteins for studying posttranscriptional events.

scholarly journals The RNA-binding Site of Bacteriophage Qβ Coat Protein

1996 ◽  
Vol 271 (50) ◽  
pp. 31839-31845 ◽  
Author(s):  
Francis Lim ◽  
Marc Spingola ◽  
David S. Peabody
Keyword(s):  
Coat Protein ◽  
Binding Site ◽  
Rna Binding

Mutational and Structural Analysis of the RNA Binding Site for Escherichia coli Ribosomal Protein S7

1994 ◽  
Vol 244 (1) ◽  
pp. 74-85 ◽  
Author(s):  
François Dragon ◽  
Catherine Payant ◽  
Léa Brakier-Gingras
Keyword(s):  
Escherichia Coli ◽  
Structural Analysis ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Rna Binding
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