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PubMed1994

Separate detection of the two complementary RNA strands of hepatitis A virus.

The minus strand of hepatitis A virus can be detected specifically by reverse transcription and polymerase chain reaction amplification in infected cell culture extracts. Several controls gave evidence that the amplified fragment actually used the minus strand as initial template. Non-thermostable reverse transcriptase was not efficient for this purpose because of self-priming of the positive-stranded viral RNA during the reverse transcription step. This problem was overcome by the use of the thermostable rTth DNA polymerase that also has reverse transcriptase activity in the presence of Mn2+.

Avian Myeloblastosis Virus↗
PubMed1997

N-ethylmaleimide (NEM) can significantly improve in situ hybridization results using 35S-labeled oligodeoxynucleotide or complementary RNA probes.

We predicted that a significant source of background labeling after in situ hybridization (ISH) using 35S-labeled probes is attributable to a chemical reaction between the phosphorothioate moiety of the probe [O3P = S] and disulfides in tissue. These covalent bonds would immobilize probe in the tissue, thereby increasing background labeling. On the basis of this view, we have explored the use of N-ethylmaleimide (NEM) to irreversibly alkylate the phosphorothioate moiety of the probe and/or to alkylate free sulfhydryls in tissue to block the formation of disulfides as a method of reducing background labeling. We report that NEM can significantly decrease background labeling of 35S-labeled oligodeoxynucleotide or cRNA probes but does not affect specific labeling. We conclude that the use of NEM in ISH protocols, as outlined here, may be an additional element researchers may consider to improve the signal-to-noise ratio.

Brain Chemistry↗
PubMed2000

[Generation of Kruppel phenocopies by injecting into Drosophila embryos RNA complementary to mRNA in parallel orientation].

RNA preparations synthesized in vitro were used to study the influence of RNA interference on the Kruppel gene activity in Drosophila embryos. RNA complementary in parallel orientation to the mRNA fragment proved to induce the development of Kruppel phenocopies. The data obtained indicate that mechanisms of specific regulation of gene activity exist in Drosophila cells, which are sensitive to the formation of both parallel and antiparallel RNA-RNA duplexes that include mRNA of the corresponding gene.

Animals↗
PubMed1986

Engineering of the mRNA-interfering complementary RNA immune system against viral infection.

Creation of an artificial mRNA-interfering complementary RNA (micRNA) immune system, utilizing anti-sense RNAs to inhibit viral gene expression, has been shown to be an effective way to prevent viral infection. In the RNA coliphage SP, the gene for the maturation protein was found to be the best target for this type of immune system; mRNA-interfering complementary RNAs specific to the genes for coat protein and replicase were less effective in preventing infection. The greatest inhibitory effect was observed with a 240-base sequence encompassing the 24-base noncoding region of the maturation gene plus the 216-base coding sequence. Significantly, even a 19-base sequence covering only the Shine-Dalgarno sequence (ribosome-binding region) without the coding region exerted a strong inhibitory effect on phage proliferation. In contrast to the highly specific action against phage SP exhibited by the longer mRNA-interfering complementary RNA, the specificity with the shorter mRNA-interfering complementary RNA was broadened to phages Q beta and GA as well as SP, all of which are classified in the different groups of RNA coliphages. Therefore, this type of anti-viral reagent may be designed to have a particular breadth of specificity, thus increasing its value in various research and possibly clinical applications.

Base Sequence↗
PubMed1989

Angiotensin 'antipeptides': (-)messenger RNA complementary to human angiotensin II (+)messenger RNA encodes an angiotensin receptor antagonist.

(-)mRNA complementary to human angiotensin II (+)mRNA encodes the 'antipeptide' Glu-Gly-Val-Tyr-Val-His-Pro-Val which is structurally related to angiotensin II. Angiotensin II 'antipeptide' (antiANG II) and the desglutamyl heptapeptide (antiANG III) are Type I antagonists which inhibit the contractile action of angiotensin at smooth muscle receptors by binding to a negative modulatory site on the angiotensin receptor which is distinct from the angiotensin binding site. These findings may illustrate that the inhibitory binding site on the angiotensin receptor exists to accomodate a naturally occurring inhibitor(s), which is encoded by the DNA strand complementary to that encoding angiotensin II.

Amino Acid Sequence↗
PubMed1994

An amino acid change in the non-structural NS2 protein of an influenza A virus mutant is responsible for the generation of defective interfering (DI) particles by amplifying DI RNAs and suppressing complementary RNA synthesis.

The mutated non-structural NS2 protein of an influenza A virus mutant, Wa-182, has been shown to be responsible for the production of defective interfering (DI) particles lacking the PA gene after a single cycle high-multiplicity infection. Using a subclone of Wa-182, A3/e-3, that inherited the Wa-182 phenotype but contained only a marginal amount of DI RNAs derived from the PA gene, we showed that replication of the PA genome RNA was suppressed primarily at the step of complementary RNA (cRNA) synthesis. On the other hand, the small amounts of DI RNA species present in the stock of A3/e-3 were shown to be replicated efficiently. These findings suggested that the suppression of cRNA synthesis of the PA gene was caused by preferential amplification of the DI RNAs. The suppression of PA gene cRNA synthesis subsequently resulted in suppression of both virion RNA synthesis and secondary transcription of the PA gene. Such aberrant replication of the PA gene was found to be attributable to an amino acid change in the NS2 protein at position 32, from isoleucine to threonine. These results suggest that the NS2 protein plays a role in promoting normal replication of the genomic RNAs by preventing the replication of short-length RNA species.

Cell Line↗
PubMed1992

Antagonist effect of a receptor-mimicking peptide encoded by human angiotensin II complementary RNA.

This article reports on the binding and the angiotensin II (Ang II) antagonistic properties of a peptide, referred to as hIIA, encoded by an RNA strand complementary to the human Ang II messenger RNA. Although Ang II and hIIA (H2N-Glu-Gly-Val-Tyr-Val-His-Pro-Val-COOH) share four amino acids, the iodinated and tritiated forms of hIIA were unreactive with seven monoclonal antibodies defining four distinct epitopes on the Ang II molecule and failed to bind to Ang II hepatic and mesangial receptors. However, hIIA did inhibit binding of 125I-Ang II to rat hepatocyte membranes (IC50, 2 x 10(-7) M) and to the various monoclonal antibodies. The lowest IC50 (5 x 10(-7) M) was measured with the monoclonal antibody specific for the Ang II sequence generally considered as implicated in receptor recognition. As predicted from the binding studies, hIIA was further shown to antagonize some biological properties of Ang II. On mesangial cells, hIIA alone had no effect on intracellular calcium concentration ([Ca2+]i) and prostaglandin E2 synthesis but did abolish the transient increase in [Ca2+]i in response to 100 nM Ang II and did induce a specific dose-dependent inhibition of the Ang II-stimulated prostaglandin E2 release. Furthermore, intravenous infusion of hIIA (200 micrograms.kg-1.min-1) inhibited by 66 +/- 3% the rat hypertensive response to 100 ng.kg-1 Ang II but had no effect on the pressor activity of agents such as alpha 1-adrenergic and HT2 serotonin agonists. Our data suggest that the "complementary" peptide hIIA interacts directly with Ang II by mimicking the Ang II complementary site on the receptor and can inhibit the physiological effects of Ang II. This type of Ang II complementary peptide may serve as a model for a new class of antihypertensive drugs.

Amino Acid Sequence↗
PubMed1983

Detection of RNA complementary to herpes simplex virus in human oral squamous cell carcinoma.

Biopsy specimens from patients with oral squamous cell carcinoma were examined by in situ hybridisation for evidence of RNA complementary to herpes simplex virus (HSV) type 1, HSV type 2, and adenovirus type 2. RNA complementary to HSV was found in 66% of carcinomas and 33% of non-malignant lesions from other patients. In a further study with internally paired controls, RNA complementary to HSV was found in 53% of carcinoma biopsy specimens but in no biopsy specimens of normal oral mucosa from the same patients. RNA complementary to HSV was found in over 50% of oral squamous cell carcinomas.

Adenoviruses, Human↗
PubMed1984

A unique mechanism regulating gene expression: translational inhibition by a complementary RNA transcript (micRNA).

The expression of the genes for the major outer membrane proteins OmpF and OmpC are osmoregulated. The ompC locus was found to be transcribed bidirectionally under conditions of high osmolarity and a 174-base transcript encoded upstream of ompC was found to inhibit the OmpF production and to substantially reduce the amount of the ompF mRNA. This RNA [mRNA-interfering complementary RNA (micRNA)] has a long sequence that is complementary to the 5' end region of the ompF mRNA. We propose that the micRNA inhibits the translation of the ompF mRNA by hybridizing with it. This RNA interaction may cause premature termination of the transcription of the ompF gene or destabilization of the ompF mRNA or both.

Bacterial Outer Membrane Proteins↗
PubMed1991

Complexes formed by complementary RNA stem-loops. Their formations, structures and interaction with ColE1 Rom protein.

Regulation of replication of plasmid ColE1 involves interaction of two plasmid-specified RNA transcripts. One of these RNAs (RNA II) serves as a primer for DNA synthesis, and the other (RNA I) is complementary to part of RNA II. The complementary regions of RNA I and RNA II form several stem-loop structures. Binding of these RNAs that regulates DNA replication begins by interaction at the loop regions. Plasmid-coded Rom protein stabilizes the product of the interaction. In this paper, the mechanism of the loop-to-loop interaction between pairs of RNA stem-loops having various nucleotide sequences is studied. Binding of two stem-loops containing six to eight nucleotides in their loops requires that the loop sequences be complementary, whereas the stem sequences need not be. The association rate constants for binding of complementary pairs with various sequences are relatively similar, around 1 x 10(6) M-1 S-1. On the other hand, the rates of dissociation of the complexes vary greatly depending on the loop sequence, even for complexes having the same base composition, suggesting a strong effect of base-stacking. All the complementary bases in the seven-nucleotide loops participate in complex formation, and the resulting complex is bent a little at the interacting region. Rom binds and stabilizes any complex formed by pairs containing fully complementary loop sequences. Structures are proposed for the RNA complexes with and without Rom.

Bacterial Proteins↗
PubMed1963

Complementary RNA in nucleus and cytoplasm of mouse liver cells.

The rapidly labeled RNA from both the nuclei and cytoplasm of mouse liver cells can be bound specifically to mouse DNA. The bound fraction differs in base composition and metabolic stability from the bulk RNA. There is considerable cross reaction between this RNA and the DNA obtained from calf thymus.

Animals↗