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1.
Exon sequences distant from the splice junction are required for efficient self-splicing of the Tetrahymena IVS.
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S A Woodson 《Nucleic acids research》1992,20(15):4027-4032
The presence of a natural rRNA secondary structure element immediately preceding the 5' splice site of the Tetrahymena IVS can inhibit self-splicing by competing with base pairing between the 5' exon and the guide sequence of the IVS (P1). Formation of this alternative hairpin is preferred in short precursor RNAs, and results in loss of G-addition to the 5' splice site. Pre-rRNAs which contain longer exons of ribosomal sequence, however, splice rapidly. As many as 146 nucleotides of the 5' exon and 86 nucleotides of the 3' exon are required for efficient self-splicing of Tetrahymena precursors. The presence of nucleotides distant from the 5' splice site apparently alters the equilibrium between the alternative hairpins, and promotes formation of active precursors. This effect is dependent on the specific sequences of the ribosomal pre-RNA, since point mutations within this region reduce the rate of splicing as much as 50-fold. This system provides an opportunity to study the way in which long-range interactions can influence splice site selection in a highly structured RNA. 相似文献
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The metabolic and cardiovascular responses to two bronchiolar selective beta-adrenergic drugs, carbuterol (CAR) and salbutamol (SAL), were compared with isoproterenol (ISO) and metaproterenol (MET) in fasted, anesthetized baboons. ISO was more active than the selective beta-adrenergic drugs in elevating plasma levels of glucose, lactate, free fatty acids, insulin, and glucagon. Moreover, ISO was more active in increasing heart rate and respiratory rate and in depressing diastolic blood pressure. Although ISO was shown to have greater activity than CAR, MET, and SAL, the bronchiolar selective drugs (CAR and SAL) did produce significant changes in plasma levels of metabolic substrates and pancreatic hormones and in cardiovascular measurements at higher dose rates. 相似文献
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Checchio Mirela Vantini de Cássia Alves Rita de Oliveira Kevein Ruas Moro Gustavo Vitti Santos Durvalina Maria Mathias dos Gratão Priscila Lupino 《Journal of plant research》2021,134(6):1279-1289
Journal of Plant Research - Salinity has become one of the major factors limiting agricultural production. In this regard, different cost-effective management strategies such as the use of plant... 相似文献
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Alves Leticia Rodrigues Rossatto Davi Rodrigo Rossi Mônica Lanzoni Martinelli Adriana Pinheiro Gratão Priscila Lupino 《Protoplasma》2020,257(2):597-605
Protoplasma - The application of Se to plants growing under Cd contamination may become an alternative strategy to minimize Cd damage. However, there is no specific information available regarding... 相似文献
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The Sm-like protein Hfq is required for gene regulation by small RNAs (sRNAs) in bacteria and facilitates base pairing between sRNAs and their mRNA targets. The proximal and distal faces of the Hfq hexamer specifically bind sRNA and mRNA targets, but they do not explain how Hfq accelerates the formation and exchange of RNA base pairs. Here, we show that conserved arginines on the outer rim of the hexamer that are known to interact with sRNA bodies are required for Hfq’s chaperone activity. Mutations in the arginine patch lower the ability of Hfq to act in sRNA regulation of rpoS translation and eliminate annealing of natural sRNAs or unstructured oligonucleotides, without preventing binding to either the proximal or distal face. Stopped-flow FRET and fluorescence anisotropy show that complementary RNAs transiently form a ternary complex with Hfq, but the RNAs are not released as a double helix in the absence of rim arginines. RNAs bound to either face of Hfq quench the fluorescence of a tryptophan adjacent to the arginine patch, demonstrating that the rim can simultaneously engage two RNA strands. We propose that the arginine patch overcomes entropic and electrostatic barriers to helix nucleation and constitutes the active site for Hfq’s chaperone function. 相似文献
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Folding of RNA into an ordered, compact structure requires substantial neutralization of the negatively charged backbone by positively charged counterions. Using a native gel electrophoresis assay, we have examined the effects of counterion condensation upon the equilibrium folding of the Tetrahymena ribozyme. Incubation of the ribozyme in the presence of mono-, di- and trivalent ions induces a conformational state that is capable of rapidly forming the native structure upon brief exposure to Mg2+. The cation concentration dependence of this transition is directly correlated with the charge of the counterion used to induce folding. Substrate cleavage assays confirm the rapid onset of catalytic activity under these conditions. These results are discussed in terms of classical counterion condensation theory. A model for folding is proposed which predicts effects of charge, ionic radius and temperature on counterion-induced RNA folding transitions. 相似文献
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Effect of transcription on folding of the Tetrahymena ribozyme 总被引:1,自引:0,他引:1
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Folding mechanism of the Tetrahymena ribozyme P4-P6 domain 总被引:2,自引:0,他引:2
Synchrotron X-ray-dependent hydroxyl radical footprinting was used to probe the folding kinetics of the P4-P6 domain of the Tetrahymena group I ribozyme, which forms a stable, closely packed tertiary structure. The 160-nt domain folds independently at a similar rate (approximately 2 s(-1)) as it does in the ribozyme, when folding is measured in 10 mM sodium cacodylate and 10 mM MgCl(2). Surprisingly, tertiary interactions around a three-helix junction (P5abc) within the P4-P6 domain fold at least 25 times more rapidly (k >/= 50 s(-1)) in isolation, than when part of the wild-type P4-P6 RNA. This difference implies that long-range interactions in the P4-P6 domain can interfere with folding of P5abc. P4-P6 was observed to fold much faster at higher ionic strength than in 10 mM sodium cacodylate. Analytical centrifugation was used to measure the sedimentation and diffusion coefficients of the unfolded RNA. The hydrodynamic radius of the RNA decreased from 58 to 46 A over the range of 0-100 mM NaCl. We propose that at low ionic strength, the addition of Mg(2+) causes the domain to collapse to a compact intermediate where P5abc is trapped in a non-native structure. At high ionic strength, the RNA rapidly collapses to the native structure. Faster folding most likely results from a different average initial conformation of the RNA in higher salt conditions. 相似文献