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A System for Studying the Specificity of Serylation with Yeast Seryl-tRNA Synthetase

Ivana Weygand-Đurašević ; Department of Biochemistry, Faculty of Science, University of Zagreb, HR-10 000 Zagreb, Croatia

Puni tekst: engleski pdf 21.010 Kb

str. 451-465

preuzimanja: 177



Serylation is the covalent attachment of serine to a serine specific tRNA. It is catalyzed by the seryl-tRNA synthetase (SerRS). There are presumably two seryl-tRNA synthetases, encoded by different nuclear genes, that perform the serylation task in Saccharomyces cerevisiae. One works in the cytoplasm and the other in mitochondria. The gene for the cytoplasmic enzyme has been cloned, sequenced and can be functionally expressed both in yeast and in Escherichia coli. Its protein product is a 106 kD homodimer, which can be easily purified from bacterial and yeast overproducing strains. The enzyme recognizes six tRNASer isoacceptors and se- lenocysteine tRNA in yeast, as well as several non homologous tRNAs from prokaryotic and eukaryotic sources. By combining genetic and biochemical methods, a system for studying the recognition between yeast seryl-tRNA synthetase and tRNA substrates, both in vivo and in vitro, has been designed.

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