RNA Strands (rna + strand)

Distribution by Scientific Domains


Selected Abstracts


HCV RNA-dependent RNA polymerase replicates in vitro the 3, terminal region of the minus-strand viral RNA more efficiently than the 3, terminal region of the plus RNA

FEBS JOURNAL, Issue 22 2001
Sandrine Reigadas
The NS5B protein, or RNA-dependent RNA polymerase of the hepatitis virus type C, catalyzes the replication of the viral genomic RNA. Little is known about the recognition domains of the viral genome by the NS5B. To better understand the initiation of RNA synthesis on HCV genomic RNA, we used in vitro transcribed RNAs as templates for in vitro RNA synthesis catalyzed by the HCV NS5B. These RNA templates contained different regions of the 3, end of either the plus or the minus RNA strands. Large differences were obtained depending on the template. A few products shorter than the template were synthesized by using the 3, UTR of the (+) strand RNA. In contrast the 341 nucleotides at the 3, end of the HCV minus-strand RNA were efficiently copied by the purified HCV NS5B in vitro. At least three elements were found to be involved in the high efficiency of the RNA synthesis directed by the HCV NS5B with templates derived from the 3, end of the minus-strand RNA: (a) the presence of a C residue as the 3, terminal nucleotide; (b) one or two G residues at positions +2 and +3; (c) other sequences and/or structures inside the following 42-nucleotide stretch. These results indicate that the 3, end of the minus-strand RNA of HCV possesses some sequences and structure elements well recognized by the purified NS5B. [source]


Rubber tree (Hevea brasiliensis) trunk phloem necrosis: aetiological investigations failed to confirm any biotic causal agent

FOREST PATHOLOGY, Issue 1 2007
F. Pellegrin
Summary Trunk phloem necrosis (TPN) is currently a main constraint in rubber (Hevea brasiliensis) plantations. The apparent spread of the disease, from tree to tree along the planting line, strongly supported the implication of a pathogen that could be transmitted mechanically via the tapping knife. In order to detect a causal agent of the disease, studies focusing on characterization of the known mechanically transmitted pathogens (e.g. viroids, cryptic viruses or phytoplasma) were initiated. RNA strands of low molecular weight (200,400 and >500 bp) displaying structural similarities with viroids and viral dsRNAs were observed in various tested samples. However, attempts to show the potential role of these RNA molecules in the spread of the disease failed. First of all, there was no significant or reproducible correlation between the health status of the rubber trees sampled and these RNA molecules. Moreover, no sequence homology with known pathogens could be found when randomly amplified cDNA fragments isolated from trees presenting the disease symptoms were sequenced. In conclusion, the aetiological investigations, in order to show the presence of a pathogen responsible of the TPN disease, were non-conclusive, which tends to disprove the hypothesis of a biotic causal agent. [source]


The emerging role of microRNAs in immune cell development and differentiation

APMIS, Issue 9 2009
TIE-JUN LIANG
MicroRNAs (miRNAs) are small RNA strands (20,25 nucleotides) that regulate gene expression by translational repression as well as by messenger RNA degradation. This review will examine the application and function of miRNAs in immune cell development and differentiation. [source]


C5-Functionalized LNA: Unparalleled Hybridization Properties and Enzymatic Stability

CHEMBIOCHEM, Issue 17 2009
Michael E. Østergaard
The best of both worlds: C5-functionalized locked nucleic acids (LNAs) synergistically combine the beneficial features of C5-alkynyl DNAs and conventional antisense LNA,they are straightforward to make and yet exhibit unparalleled thermal affinity toward RNA targets, extraordinary discrimination of singly mismatched RNA strands, and superb stability against degradation by 3,-exonucleases. [source]


Oligonucleotide N3,,P5, Phosphoramidates and Thio -Phoshoramidates as Potential Therapeutic Agents

CHEMISTRY & BIODIVERSITY, Issue 3 2010
Sergei
Abstract Nucleic acids analogues, i.e., oligonucleotide N3,,P5, phosphoramidates and N3,,P5, thio -phosphoramidates, containing 3,-amino-3,-deoxy nucleosides with various 2,-substituents were synthesized and extensively studied. These compounds resist nuclease hydrolysis and form stable duplexes with complementary native phosphodiester DNA and, particularly, RNA strands. An increase in duplexes' melting temperature, ,Tm, relative to their phosphodiester counterparts, reaches 2.2,4.0° per modified nucleoside. 2,-OH- (RNA-like), 2,- O -Me-, and 2,- ribo -F-nucleoside substitutions result in the highest degree of duplex stabilization. Moreover, under close to physiological salt and pH conditions, the 2,-deoxy- and 2,-fluoro-phosphoramidate compounds form extremely stable triple-stranded complexes with either single- or double-stranded phosphodiester DNA oligonucleotides. Melting temperature, Tm, of these triplexes exceeds Tm values for the isosequential phosphodiester counterparts by up to 35°. 2,-Deoxy-N3,,P5, phosphoramidates adopt RNA-like C3,- endo or N -type nucleoside sugar-ring conformations and hence can be used as stable RNA mimetics. Duplexes formed by 2,-deoxy phosphoramidates with complementary RNA strands are not substrates for RNase H-mediated cleavage in vitro. Oligonucleotide phosphoramidates and especially thio -phosphoramidates conjugated with lipid groups are cell-permeable and demonstrate high biological target specific activity in vitro. In vivo, these compounds show good bioavailability and efficient biodistribution to all major organs, while exerting acceptable toxicity at therapeutically relevant doses. Short oligonucleotide N3,,P5, thio -phosphoramidate conjugated to 5,-palmitoyl group, designated as GRN163L (Imetelstat), was recently introduced as a potent human telomerase inhibitor. GRN163L is not an antisense agent; it is a direct competitive inhibitor of human telomerase, which directly binds to the active site of the enzyme and thus inhibits its activity. This compound is currently in multiple Phase-I and Phase-I/II clinical trials as potential broad-spectrum anticancer agent. [source]