Site-specific cleavage of tRNA by imidazole and/or primary amine groups bound at the 5′-end of oligodeoxyribonucleotides

Ushijima, Kaoru; Gouzu, Hidetaka; Hosono, Kuniaki; Shirakawa, Masahiro; Kagosima, Koumei; Takai, Kazuyuki; Takaku, Hiroshi

doi:10.1016/s0304-4165(97)00101-3

Cited by 37 publications

(19 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This oligonucleotide contains two histamine groups conjugated through carbamate linkages to a tris(2-aminoethyl) tether that is attached to the 2′-position of an internal ribonucleotide. This functional group, when attached to the 5′-end of antisense oligonucleotide has been shown to effectively catalyze hydrolysis of tRNA [11] . Hybridization of oligo-7 to RNA-1 or RNA-2 creates duplexes that contain a 1 or 2 nucleotide bulge respectively in the RNA target.…”

Section: Resultsmentioning

confidence: 99%

Hydrolysis of Bulged Nucleotides in Hybrids Formed by Rna and Imidazole-Derivatized Oligo-2′-O-Methylribonucleotides

Saleh

Miller

2011

Nucleosides, Nucleotides and Nucleic Acids

View full text Add to dashboard Cite

In order to enhance the efficacy of small antisense molecules, we examined a series of antisense oligonucleotides derivatized with functional groups designed to enable them to hydrolyze their RNA target. Solid phase synthetic methods were used to prepare imidazole-derivatized antisense oligo-2′-O-methylribonucleotides. Upon binding, these oligonucleotides create internal bulged bases in the target RNA that serve as sites for hydrolysis. We observed that an oligonucleotide derivatized with a side chain containing two imidazole groups was capable of hydrolyzing 58% of its RNA target when incubated with the target for 48 hours at 37°C and physiological pH.

show abstract

Section: Resultsmentioning

confidence: 99%

Hydrolysis of Bulged Nucleotides in Hybrids Formed by Rna and Imidazole-Derivatized Oligo-2′-O-Methylribonucleotides

Saleh

Miller

2011

Nucleosides, Nucleotides and Nucleic Acids

View full text Add to dashboard Cite

show abstract

“…The RNA–OAS–resin complex was washed with 100 μl of the same buffer supplemented with 250 mM potassium chloride followed by two washes with 500 μl of OAS buffer minus EDTA. The RNA–OAS complex was removed from the resin by adding 250 μl strip buffer [20 mM Tris–HCl (pH 8.0), 100 mM sodium chloride and 100 mM EDTA] in DEPC-treated H 2 O. Imidazole was not used due to possible site-specific cleavage of RNAs (39). The supernatant was added to 250 μl of protein digestion buffer [50 mM Tris–HCl (pH 7.5), 5 mM calcium chloride and 0.5% SDS] and treated with 100 μg/ml Proteinase K (Promega Corp., Madison, WI, USA) at 37°C for 90 min.…”

Section: Methodsmentioning

confidence: 99%

Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2′,5′-oligoadenylate synthetase from prostate cancer cells

Molinaro

Jha

Malathi

et al. 2006

Nucleic Acids Research

View full text Add to dashboard Cite

The antiviral and antitumor functions of RNase L are enabled by binding to the allosteric effectors 5′-phosphorylated, 2′,5′-linked oligoadenylates (2-5A). 2-5A is produced by interferon-inducible 2′,5′-oligoadenylate synthetases (OAS) upon activation by viral double-stranded RNA (dsRNA). Because mutations in RNase L have been implicated as risk factors for prostate cancer, we sought to determine if OAS activators are present in prostate cancer cells. We show that prostate cancer cell lines (PC3, LNCaP and DU145), but not normal prostate epithelial cells (PrEC), contain RNA fractions capable of binding to and activating OAS. To identify the RNA activators, we developed a cDNA cloning strategy based on stringent affinity of RNAs for OAS. We thus identified mRNAs for Raf kinase inhibitor protein (RKIP) and poly(rC)-binding protein 2 (PCBP2) that bind and potently activate OAS. In addition, human endogenous retrovirus (hERV) envelope RNAs were present in PC3 cells that bind and activate OAS. Analysis of several gene expression profiling studies indicated that PCBP2 RNA was consistently elevated in metastatic prostate cancer. Results suggest that OAS activation may occur in prostate cancer cells in vivo stimulated by cellular mRNAs for RKIP and PCBP2.

show abstract

“…Conjugation of various catalysts (other lanthanide(III) complexes, multi-nuclear metal complexes, or organic molecular scissors in Fig. (2) and (3) with DNA oligomers was also effective for site-selective RNA scission [24][25][26][27][28][29][30][31][32][33][34].…”

Section: Covalent Artificial Ribonucleasesmentioning

confidence: 99%

Site-Selective Artificial Ribonucleases and their Applications

Kuzuya¹,

Komiyama

2007

COC

View full text Add to dashboard Cite

Recent developments in artificial enzymes for site-selective scission of RNA have been reviewed, and their advantages over ribozymes are discussed. Most of previous reports involve covalent fixation of molecular scissors to sequence-recognizing moieties. However, non-covalent strategy, in which these two components are never covalently bound each other, has made remarkable progresses. When oligonucleotide bearing an acridine (site-selective activator) forms duplex with RNA substrate, the phosphodiester linkage of the RNA in front of the acridine is selectively activated and hydrolyzed by various metal ions (e.g., Lu(III). These non-covalent artificial ribonucleases are simple enough to be used for various more complicated systems. For example, tandem activator for clipping of desired fragment from long RNA substrate is obtained by attaching two acridines to an oligonucleotide. By analyzing the resultant RNA fragment with MALDI-TOFMS, the RNA substrate is accurately genotyped in terms of both single nucleotide polymorphisms (SNPs) and insertion/deletion polymorphisms (Indels).

show abstract

Site-specific cleavage of tRNA by imidazole and/or primary amine groups bound at the 5′-end of oligodeoxyribonucleotides

Cited by 37 publications

References 26 publications

Hydrolysis of Bulged Nucleotides in Hybrids Formed by Rna and Imidazole-Derivatized Oligo-2′-O-Methylribonucleotides

Hydrolysis of Bulged Nucleotides in Hybrids Formed by Rna and Imidazole-Derivatized Oligo-2′-O-Methylribonucleotides

Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2′,5′-oligoadenylate synthetase from prostate cancer cells

Site-Selective Artificial Ribonucleases and their Applications

Contact Info

Product

Resources

About