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Magnesium-dependent alternative foldings of active and inactive Escherichia coli tRNA(Glu) revealed by chemical probing
- Source :
- Nucleic acids research. 27(17)
- Publication Year :
- 1999
-
Abstract
- A stable conformer of Escherichia coli tRNA(Glu), obtained in the absence of Mg(2+), is inactive in the aminoacylation reaction. Probing it with diethylpyrocarbonate, dimethyl sulfate and ribonuclease V1 revealed that it has a hairpin structure with two internal loops; the helical segments at both extremities have the same structure as the acceptor stem and the anticodon arm of the native conformer of tRNA(Glu)and the middle helix is formed of nucleotides from the D-loop (G15-C20:2) and parts of the T-loop and stem (G51-C56), with G19 bulging out. This model is consistent with other known properties of this inactive conformer, including its capacity to dimerize. Therefore, this tRNA requires magnesium to acquire a conformation that can be aminoacylated, as others require a post-transcriptional modification to reach this active conformation.
- Subjects :
- Alkylating Agents
Protein Denaturation
Adenosine
Stereochemistry
Aminoacylation
Biology
Sulfuric Acid Esters
medicine.disease_cause
Dimethyl sulfate
chemistry.chemical_compound
Cytosine
Diethyl Pyrocarbonate
Endoribonucleases
Genetics
medicine
Escherichia coli
Nucleotide
Magnesium
Conformational isomerism
chemistry.chemical_classification
Ribonuclease V1
RNA, Transfer, Glu
chemistry
Biochemistry
Transfer RNA
Helix
Nucleic Acid Conformation
Research Article
Subjects
Details
- ISSN :
- 13624962
- Volume :
- 27
- Issue :
- 17
- Database :
- OpenAIRE
- Journal :
- Nucleic acids research
- Accession number :
- edsair.doi.dedup.....be88113d32bdd82479b8e3e10e422876