Protein-RNA molecular recognition
Article Abstract:
The conflict between in vitro and in vivo studies on the role of the G*U base pair of the Escherichia coli alanyltransfer RNA (tRNA(super Ala)) in protein-RNA recognition can be resolved by determining the structure of tRNA(super Ala) and alanyl-tRNA synthetase complex. In vitro studies suggest that G*U permits direct recognition of the RNA helix minor groove. In vivo studies indicate that G.U helps in tRNA(super Ala) and alanyl-tRNA synthetase interaction. Both studies suffer from experimental assumptions and limitations, and their results may be incorrect.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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tRNA-dependent asparagine formation
Article Abstract:
The transamidation, rather than the acylation, of Asp-tRNA(super Asn) mediates the formation of asparaginyl-tRNA (super Asn) in Haloferax volcanii. Total tRNA is less well charged by glutamine than by glutaminyl in the presence of dialysed S100 extract. Asparaginyl substrate has lesser influence than asparagine in tRNA aminoacylation, indicating that asparaginyl is unlikely to activate tRNA synthetase activity.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Domain-specific recruitment of amide amino acids for protein synthesis
Article Abstract:
All archaea are found to have an archaea-specific heterodimeric amidotransferase, although Asn-tRNA synthesis in archaea is divergent.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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