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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Madore E,Florentz C,Giegé R,Lapointe Jdoi
10.1093/nar/27.17.3583keywords:
subject
Has Abstractpub_date
1999-09-01 00:00:00pages
3583-8issue
17eissn
0305-1048issn
1362-4962pii
gkc521journal_volume
27pub_type
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