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Specificity of the photo reaction of 4' hydroxymethyl 4 5' 8 trimethyl psoralen with rna identification of reactive sites in escherichia coli phenyl alanine accepting transfer rna






Biochemistry 21(6): 1357-1363

Specificity of the photo reaction of 4' hydroxymethyl 4 5' 8 trimethyl psoralen with rna identification of reactive sites in escherichia coli phenyl alanine accepting transfer rna

To test the potential of psoralen photoaddition for the probing of RNA conformation at sequence resolution, the specificity of the reaction of 4'-(hydroxymethyl)-4,5',8-trimethylpsoralen (HMT) with E. coli tRNAPhe was analyzed. The sites of HMT covalent addition were identified by a combination of analytical techniques involving chemical cleavage of the tRNAPhe molecule at the m7G [7-methylguanine] site and gel electrophoresis of RNase T1 digests together with paper electrophoretic characterization of HMT-modified nucleotides and oligonucleotides. Advantage was taken of the alteration of the cleavage rate of pancreatic RNase adjacent to a photoadduct. HMT photoaddition showed a very high preference for uracil residues. Important differences in HMT photoreactivity were observed for various U sites of the tRNAPhe molecule. Reactivity of specific bases was correlated with partial melting of the molecule. There appears to be a strong preference of the photoreactive probe for a loose helical conformation as compared with a tight helix, whereas a random coil appears poorly reactive.


Accession: 006459109



Related references

Bachellerie J P.; Hearst J.E., 1980: Identification of hydroxymethyl trimethyl psoralen binding sites in escherichia coli phenyl alanyl transfer rna. Federation Proceedings 39(6): ABSTRACT 2194

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Turner, S.; Noller, H.F., 1983: Identification of sites of 4' hydroxymethyl 4 5' 8 trimethyl psoralen cross linking in escherichia coli 23s ribosomal rna. The reagent 4'-(hydroxymethyl)-4,5',8-trimethylpsoralen (HMT) was used to cross-link 23S rRNA from E. coli under 50S ribosomal subunit reconstitution conditions. Following partial digestion of the RNA with RNase T1, 2-dimensional diagnoa...

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Yarus M., 1972: Solvent and specificity binding and iso leucylation of phenyl alanine transfer rna escherichia coli by iso leucyl transfer rna synthetase from escherichia coli. Biochemistry: 2352-2361

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Robbins, D.; Odom, O.W.Jr ; Lynch, J.; Kramer, G.; Hardesty, B.; Liou, R.; Ofengand, J., 1981: Position of transfer rna on escherichia coli ribosomes distance from the 3' end of 16s rna to 3 points on phenyl alanine accepting transfer rna in the donor site of 70s ribosomes. E.coli 16S RNA from 30S ribosomal subunits was isolated, oxidized at the 3' end, and labeled with the thiosemicarbazide derivatives of fluorescein or eosin. Labeled 16S RNA was reconstituted into 30S subunits. They were almost fully active co...

Knorre D.G.; Lavrik O.I.; Prudchenko A.T., 1970: Investigation of the specificity of phenyl alanyl transfer rna synthetase from escherichia coli mre 600 to fluorinated analogs of phenyl alanine. Doklady Akademii Nauk SSSR Seriya Biologiya 195(3): 735-737

Prudchenko A.T., 1971: Investigation of the specificity of phenyl alanyl transfer rna synthetase from escherichia coli mre 600 with respect to fluorinated analogues of phenyl alanine. Doklady Akademii Nauk Sssr Biochemistry Section-6: 348-350,

Holler E.; Bartmann P.; Hanke T.; Kosakowski H.M., 1973: Phenyl alanyl transfer rna synthetase from escherichia coli synergistic coupling between the sites for binding of l phenyl alanine and atp. Biochemical & Biophysical Research Communications 53(4): 1205-1212