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Results for “RNA structure”

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At least 379 records · Page 21Linked to original sources
PubMed2005

Resolution enhanced homonuclear carbon decoupled triple resonance experiments for unambiguous RNA structural characterization.

Large RNAs (>30 nucleotides) suffer from extensive resonance overlap that can seriously hamper unambiguous structural characterization. Here we present a set of 3D multinuclear NMR experiments with improved and optimized resolution and sensitivity for aiding with the assignment of RNA molecules. In all these experiments strong base and ribose carbon-carbon couplings are eliminated by homonuclear band-selective decoupling, leading to improved signal to noise and resolution of the C5, C6, and C1' carbon resonances. This decoupling scheme is applied to base-type selective 13C-edited NOESY, 13C-edited TOCSY (HCCH, CCH), HCCNH, and ribose H1C1C2 experiments. The 3D implementation of the HCCNH experiment with both carbon and nitrogen evolution enables direct correlation of 13C and 15N resonances at different proton resonant frequencies. The advantages of the new experiments are demonstrated on a 36 nucleotides hairpin RNA from domain 5 (D5) of the group II intron Pylaiella littoralis using an abbreviated assignment strategy. These four experiments provided additional separation for regions of the RNA that have overlapped chemical shift resonances, and enabled the assignment of critical D5 bulge nucleotides that could not be assigned using current experimental schemes.

Carbon Isotopes↗
PubMed1999

RNA structure, metal ions, and catalysis.

Several new and unexpected insights into the metalloenzymology of ribozymes have been achieved in the past year. From a mechanistic point of view, the NMR and crystal structures of a small Pb(2+)-dependent ribozyme have been particularly revealing.

Catalysis↗
PubMed1986

DNA primase of human mitochondria is associated with structural RNA that is essential for enzymatic activity.

DNA primase isolated from human mitochondria sediments in glycerol density gradients at 30S and 70S. These unusually high sedimentation coefficients are a result of association of the primase activity with RNA. Treatment of primase with nuclease not only affects its sedimentation behavior, but also inactivates the primase activity. The major RNA species that cofractionates with primase activity is shown by direct sequence analysis to be cytosolic 5.8S ribosomal RNA (rRNA). Specific degradation of endogenous 5.8S rRNA using ribonuclease H and oligonucleotides complementary to 5.8S rRNA results in reduction of primase activity. Other small RNAs may play a structural role in the formation of an active DNA primase complex.

Centrifugation, Density Gradient↗
PubMed1972

Messenger RNA structure: compatibility of hairpin loops with protein sequence.

Examination of the amino acid sequences of human cytochrome c and the alpha-chain variant of human hemoglobin Constant Spring has revealed the possiblity for base-paired hairpin loops in the messenger RNA's for these proteins. A similar analysis of the bacteriophage R17 coat protein suggests an additional unobserved loop in the R17 RNA. If such loops are present in messenger RNA's generally, it would suggest that DNA has more than one stable base-paired conformation.

Amino Acid Sequence↗
PubMed1977

RNA structure.

Explore the source record for details and available documents.

Anticodon↗
PubMed1976

The multipartite genome of brome mosaic virus: aspects of in vitro translation and RNA structure.

The multipartite nature of the brome mosaic virus genome is described. Particular attention is given to the translation of the RNAs in cell-free extracts, from dry wheat seed embryos and commercial wheat germ. Such studies have demonstrated that the smallest RNA is a monocistronic message for coat protein. This cistron is also carried on the intermediate sized RNA, which also codes for a larger protein, of unknown function. Translation of the larger RNAs 1 and 2 is compared, incell-free extracts of wheat embryo and wheat germ. There is evidence that these RNAs may also be monocistronic messages for large polypeptides (molecular weight 100,000), indicating that there are few non-translatable regions on these RNAs. Some recent nucleotide sequence studies are described, including the ribosome binding site of the coat protein cistron, and the 3' termini of all four RNAs, which appear to be identical, at least over a region of 150 nucleotides.

Amino Acids↗
PubMed2002

The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR.

The dsRNA-activated protein kinase PKR is involved in signal transduction pathways that mediate cellular processes as diverse as cell growth and differentiation, the stress response, and apoptosis. PKR was originally described as an interferon-inducible elF2alpha kinase involved in the antiviral defense mechanism of the cell. The interaction of the kinase with specific viral RNAs has been studied in much detail, but information about cellular mRNAs, which are able to bind and activate PKR, is scarce. In search for such cellular mRNAs, we developed a cloning strategy to identify individual mRNA species from the dsRNA-rich fraction of Daudi cell poly(A)+ RNA. Two out of five cDNA clones we obtained contained sequences derived from the mRNA of the translationally controlled tumor protein P23/TCTP, indicating that this mRNA is present in the dsRNA-rich fraction. Secondary structure predictions and gel electrophoretic mobility investigations on P23/TCTP transcripts confirmed the potential of this mRNA to form extensive secondary structure. A full-length P23 transcript, but not a truncated version thereof, was able to bind to PKR in vitro and in vivo. Transient transfection experiments in human 293 cells showed that coexpression of full-length P23 mRNA leads to partial inhibition of the expression of a beta-galactosidase reporter gene in trans. Additional coexpression of a dominant negative mutant of PKR or of adenovirus VA1 RNA suppressed this inhibition, indicating that it is mediated by PKR. Studies on P23/TCTP expression in cells from PKR-knockout mice suggest that P23/TCTP mRNA translation is regulated by PKR. Hence, our results demonstrate that the mRNA of P23/TCTP may both activate PKR and be subject to translational regulation by this kinase.

Animals↗