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Figure 1.

Enzymatic probing (A, B, E, F) and NMR analysis (C, D, G, H, I) of miR-21 (A-D), miR-93 (E-H) and miR-296 (I).

A, B, E, F. Cleavage patterns obtained for limited hydrolysis of 5'-end labeled miR-21 (A, B) and miR-93 (E, F) with RNase V1, nuclease S1 and RNase T1 in native conditions. Lanes: C - reaction control; L – OH ladder; T1 - limited hydrolysis by RNase T1 (0.025u/µl) in denaturing condition. A. Lines V1 - limited hydrolysis with RNase V1 (0, 0.03125, 0.0625 or 0.125 u/µl). B. Lanes T1(N) - limited hydrolysis with RNase T1 (0, 0.04, 0.02 or 0.01 u/µl) in native conditions. E. Line V1 - limited hydrolysis with RNase V1 (0.125 u/µl). F. Lines S1 - limited hydrolysis with nuclease S1 (0.00475 u/µl). The increasing concentrations of RNase V1 and RNase T1 are indicated by arrows. Cleavage sites are indicated in autoradiogram. C, D, G, H, I. NMR analysis of miR-21 (C, D) miR-93 (G, H) and miR-296 (I) structures. C. The imino region of 1H NMR spectrum of miR-21 (0.7 mM) recorded at 7°C in H2O:D2O (90%:10%) with 150 mM sodium chloride, 10 mM phosphate buffer and 0.1 mM EDTA. Resonances arising from the hairpin form are indicated with *. D. Imino region of the 1H-1H 2D NOESY spectrum of miR-21 at 15°C in H2O:D2O (90%:10%) with 150 mM sodium chloride, 10 mM phosphate buffer and 0.1 mM EDTA. The lines indicate the imino proton connectivity. G. The imino region of 1H NMR spectrum of miR-93 (0.75 mM) recorded at 25°C in H2O:D2O (90%:10%) with 150 mM sodium chloride (top) or 50 mM sodium chloride (bottom), 10 mM phosphate buffer and 0.1 mM EDTA. Resonances arising from the hairpin form are indicated with *. H. Imino region of the 1H-1H 2D NOESY spectrum of miR-93 at 15°C in H2O:D2O (90%:10%) with 150 mM sodium chloride, 10 mM phosphate buffer and 0.1 mM EDTA. The lines indicate the imino proton connectivity. I. The imino region of 1H NMR spectrum of miR-296 (0.3 mM) recorded at 25°C in H2O:D2O (90%:10%) with 150 mM sodium chloride, 10 mM phosphate buffer and 0.1 mM EDTA.

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Figure 2.

Distribution of linear and nonlinear human miRNAs and of hairpin stem location in predicted human secondary structure (A); and folding distribution of human mature miRNAs strands (B).

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Figure 3.

Concentration dependency plots of miR-21, miR-93, miR-296 monomer and dimer (A) and the scheme illustrating concentration dependent equilibriums of these miRNAs (B).

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Table 1.

Some parameters of miRNAs and the partition of monomer and dimer formation in concentration dependence.

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Table 1 Expand

Figure 4.

miR-21, miR-93 and miR-296 stability in GBM lysate.

A, B. Hydrolysis of 5′-end labeled miR-21, miR-93 and miR-296 in 0.01 mg/ml GBM lysate. C. Half-lives of miR-21, miR-93 and miR-296.

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Figure 5.

Similarity of structures of miR-21, miR-93, miR-296 and anti-Tn-C aptamer TN-9.6.

A. RNA structure cluster of miR-21, miR-93, miR-296 and TN-9.6. B. ASCII representation of a consensus sequence and structure of miR-21, miR-93, miR-296 and TN-9.6. Multiple structure alignments of anti-Tn-C aptamer TN-9, its derivatives (TN-9.4, TN-9.6), miR-21 and miR-93 based. C. Graphic representation of miR-21, miR-93, miR-296 and TN-9.6 structures similarity. Regions of structures identical within compared group are marked in black. Calculations are made by RNAforester algorithms. The obtained score is 80.25.

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Figure 5 Expand