Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

D. J. Wright; S. A. Martinis; M. Jahn; D. Söll; P. Schimmel

doi:10.1016/0300-9084(93)90003-B

Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

D. J. Wright, S. A. Martinis, M. Jahn, D. Söll, P. Schimmel

Research output: Contribution to journal › Article › peer-review

Abstract

The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNA^Gln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNA^Gln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation.

Original language	English (US)
Pages (from-to)	1041-1049
Number of pages	9
Journal	Biochimie
Volume	75
Issue number	12
DOIs	https://doi.org/10.1016/0300-9084(93)90003-B
State	Published - 1993
Externally published	Yes

Keywords

RNA recognition
aminoacyl tRNA synthetases
evolution of coding
genetic code
tRNA identity

ASJC Scopus subject areas

Biochemistry

Online availability

10.1016/0300-9084(93)90003-B

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title = "Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase",

abstract = "The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNAGln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNAGln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation.",

keywords = "RNA recognition, aminoacyl tRNA synthetases, evolution of coding, genetic code, tRNA identity",

author = "Wright, {D. J.} and Martinis, {S. A.} and M. Jahn and D. S{\"o}ll and P. Schimmel",

note = "Funding Information: We are grateful to Dr JP Shi and Professor K Musier-Forsyth for donating RNA substrates and for helpful discussion. This work was supported by National Institute of Health grants GM15539 and GM23562 to PS and GM22854 to DS. SAM (1991-1993) and DJW (1991-1993) were American Cancer Society postdoctoral fellows.",

year = "1993",

doi = "10.1016/0300-9084(93)90003-B",

language = "English (US)",

volume = "75",

pages = "1041--1049",

journal = "Biochimie",

issn = "0300-9084",

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number = "12",

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T1 - Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

AU - Wright, D. J.

AU - Martinis, S. A.

AU - Jahn, M.

AU - Söll, D.

AU - Schimmel, P.

N1 - Funding Information: We are grateful to Dr JP Shi and Professor K Musier-Forsyth for donating RNA substrates and for helpful discussion. This work was supported by National Institute of Health grants GM15539 and GM23562 to PS and GM22854 to DS. SAM (1991-1993) and DJW (1991-1993) were American Cancer Society postdoctoral fellows.

PY - 1993

Y1 - 1993

N2 - The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNAGln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNAGln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation.

AB - The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNAGln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNAGln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation.

KW - RNA recognition

KW - aminoacyl tRNA synthetases

KW - evolution of coding

KW - genetic code

KW - tRNA identity

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Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

Abstract

Keywords

ASJC Scopus subject areas

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