NDLI: The 3'-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem.

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The 3'-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Limmer, S. Sprinzl, M. Hofmann, H. P. Ott, G.
Description	Author Affiliation: Limmer S ( Laboratorium für Biochemie, Universität Bayreuth, Federal Republic of Germany.);
Abstract	We have done a systematic study on the contribution of the single-stranded NCCA end (where N is any nucleotide) to the stability of the aminoacyl stem of tRNA. A 7-bp RNA duplex with the single-strand ACCA 3' terminus derived from the aminoacyl stem of Escherichia coli tRNA(Ala) and several chemically synthesized sequence variants are characterized by proton NMR and thermodynamic parameters. The single-stranded 3' terminus noticeably stabilizes the duplex in a sequence-dependent manner. Though the largest contribution to the stability gain due to the ACCA end is provided by the first dangling 3' nucleotide, the influence of even the fourth nucleotide is measurable. The nature of the N73 discriminator base influences the stem structure and stability, which may be important for the recognition of tRNA by aminoacyl-tRNA synthetase. The stepwise attachment of the nucleotides to the 3' tail improves the stacking of the unpaired bases over the helix stem. Hence, the ACCA end appears to be structured. Replacing Mg2+ with Mn2+ causes broadening of certain imino proton peaks in the NMR spectrum, indicating a specific divalent metal ion binding site in the vicinity of the major identity element of the duplex (G3-U70) that is required for its recognition by the Ala-tRNA synthetase.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acyl-tRNA Synthetases Metabolism RNA, Bacterial Chemistry RNA, Transfer Base Composition Binding Sites Magnesium Magnetic Resonance Spectroscopy Manganese Molecular Sequence Data Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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