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Nucleic Acids Research, 1989, Vol. 17, No. 14 5725-5736
© 1989

ENZYMOLOGY

Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase

Gilbert Eriani, Guy Dirheimer and Jean Gangloff*

Institut de Biologie Molèculaire et Cellulaire du CNRS and Universitè L.Pasteur, Laboratoire de Biochimie 15 rue Ren6 Descartes, 67084 Strasbourg, France

*To whom correspondence should be addressed

Received April 24, 1989. Accepted June 23, 1989.

The gene coding for Escherichiu coli arginyl-tRNA synthetase (argS) was isolated as a fragment of 2.4 kb after analysis and subcloning of rccombinant plasmids from the Clarke and Carbon library. The clone bearing the gene overproduces arginyl-tRNA synthetase by a factor 100. This means that the enzyme represents more than 20% of the cellular total protein content. Sequencing revealed that the fragment contains a unique open reading frame of 1734 bp flanked at its 5' and 3' ends respectively by 247 bp and 397 bp. The length of the corresponding protein (577 aa) is well consistent with earlier Mr determination (about 70 kd). Primer extension analysis of the ArgRS mRNA by reverse transcriptase, located its 5' end respectively at 8 and 30 nucleotides downstream of a TATA and a TTGAC like element (CTGAC) and 60 nucleotides upstream of the unusual translation initiation codon GUG ; nuclease SI analysis located the 3'-end at 48 bp downstream of the translation termination codon. argS has a codon usage pattern typical for highly expressed E.coli genes. With the exception of the presence of a HVGH sequence similar to the HIGH consensus element, ArgRS has no relevant sequence homologies with other aminoacyl-tRNA synthetases.


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