scholarly journals Sequence analysis of an artificial family of RNA-binding peptides

2009 ◽  
Vol 11 (11) ◽  
pp. 2688-2696 ◽  
Author(s):  
Jeffrey E. Barrick ◽  
Richard W. Roberts
Keyword(s):  
Sequence Analysis ◽  
Rna Binding ◽  
Binding Peptides

Cloning and Sequence Analysis of Cold Inducible RNA-binding Protein cDNA from Testis Tissue in BALB/C Mice*

2010 ◽  
Vol 2009 (1) ◽  
pp. 87-90
Author(s):  
Fuhou JIN ◽  
Yan PANG ◽  
Shize LI ◽  
Huanmin YANG ◽  
Hong JI ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Testis Tissue

Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein

1991 ◽  
Vol 11 (6) ◽  
pp. 3075-3087
Author(s):  
L Minvielle-Sebastia ◽  
B Winsor ◽  
N Bonneaud ◽  
F Lacroute
Keyword(s):  
Molecular Weight ◽  
Sequence Analysis ◽  
Decay Rate ◽  
Rna Binding ◽  
Binding Domain ◽  
Temperature Sensitive ◽  
Multicopy Plasmid ◽  
Wild Type ◽  
Rna Binding Domain ◽  
Temperature Sensitive Phenotype

In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length. Although mRNA transcription is not abolished in these mutants, the transcripts are rapidly deadenylated as in a strain carrying an RNA polymerase B(II) temperature-sensitive mutation. This suggests that the primary defect could be in the control of the poly(A) status of the mRNAs and that the fast decay rate may be due to the loss of this control. By complementation of their temperature-sensitive phenotype, we have cloned the wild-type genes. They are essential for cell viability and are unique in the haploid genome. The RNA14 gene, located on chromosome H, is transcribed as three mRNAs, one major and two minor, which are 2.2, 1.5, and 1.1 kb in length. The RNA15 gene gives rise to a single 1.2-kb transcript and maps to chromosome XVI. Sequence analysis indicates that RNA14 encodes a 636-amino-acid protein with a calculated molecular weight of 75,295. No homology was found between RNA14 and RNA15 or between RNA14 and other proteins contained in data banks. The RNA15 DNA sequence predicts a protein of 296 amino acids with a molecular weight of 32,770. Sequence comparison reveals an N-terminal putative RNA-binding domain in the RNA15-encoded protein, followed by a glutamine and asparagine stretch similar to the opa sequences. Both RNA14 and RNA15 wild-type genes, when cloned on a multicopy plasmid, are able to suppress the temperature-sensitive phenotype of strains bearing either the rna14 or the rna15 mutation, suggesting that the encoded proteins could interact with each other.

Selection of RNA-Binding Peptides Using mRNA-Peptide Fusions

Methods ◽  
2001 ◽  
Vol 23 (3) ◽  
pp. 287-293 ◽  
Author(s):  
Jeffrey E. Barrick ◽  
Terry T. Takahashi ◽  
Andrey Balakin ◽  
Richard W. Roberts
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Selection Of

Sequence and structure space of RNA-binding peptides

Biopolymers ◽  
2003 ◽  
Vol 70 (1) ◽  
pp. 80-85 ◽  
Author(s):  
Chandreyee Das ◽  
Alan D. Frankel
Keyword(s):  
Rna Binding ◽  
Structure Space ◽  
Binding Peptides

scholarly journals N-Methylation as a Strategy for Enhancing the Affinity and Selectivity of RNA-binding Peptides: Application to the HIV-1 Frameshift-Stimulating RNA

2015 ◽  
Vol 11 (1) ◽  
pp. 88-94 ◽  
Author(s):  
Thomas A. Hilimire ◽  
Ryan P. Bennett ◽  
Ryan A. Stewart ◽  
Pablo Garcia-Miranda ◽  
Alex Blume ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Peptides ◽  
Hiv 1

Selection of RNA-binding peptides from combinatorial libraries

1996 ◽  
Vol 26 (3-5) ◽  
pp. 258-258
Author(s):  
Kazuo Harada ◽  
Shelley Martin ◽  
Alan D. Frankel
Keyword(s):  
Rna Binding ◽  
Combinatorial Libraries ◽  
Binding Peptides ◽  
Selection Of
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