Characterization of some major identity elements in plant alanine and phenylalanine transfer RNAs View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-12

AUTHORS

Vera T. C. Carneiro, André Dietrich, Laurence Maréchal-Drouard, Anne Cosset, Georges Pelletier, Ian Small

ABSTRACT

Alanine and phenylalanine tRNA sequences were amplified by PCR from Arabidopsis thaliana nuclear DNA using degenerate oligonucleotides which introduced specific mutations into the acceptor stem. The aminoacylation of T7 RNA polymerase transcripts of these sequences was investigated in vitro using partially purified bean alanyl- or phenylalanyl-tRNA synthetase. In parallel, the in vivo activity of amber suppressor derivatives of these tRNAs was investigated in transient expression assays in tobacco protoplasts using a beta-glucuronidase (GUS) reporter gene containing a premature amber stop codon. The results show that mutation of the G3:U70 base pair to G3:C70 blocks aminoacylation of plant alanine tRNA, whilst conversion of the G3:C70 pair normally found in plant tRNA(Phe) to G3:U70 enables the mutated tRNA(Phe) to be a good substrate for alanyl-tRNA synthetase and impairs its aminoacylation with phenylalanine. In addition, the amber suppressor derivative of wild-type tRNA(Phe) showed very little suppressor activity in vivo, and was poorly aminoacylated with phenylalanine in vitro, suggesting that the anticodon is a major identity determinant for tRNA(Phe) in plant cells. More... »

PAGES

1843-1853

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00019497

DOI

http://dx.doi.org/10.1007/bf00019497

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009210053

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7532029


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This table displays all metadata directly associated to this object as RDF triples.

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