Abstract
The nucleotide sequence of a 3.6-kilobase pair DNA fragment containing the structural gene for yeast cytoplasmic lysyl-tRNA synthetase (KRS1) and its flanking regions was determined. The encoded protein of 67,881 kDa displays a cluster of 11 lysines within a 29-amino acid residue segment at its amino-terminal extremity. Evidence is presented that this segment is responsible for the affinity displayed by the native enzyme toward polyanionic carriers. The transcription initiation sites of the KRS1 gene were determined. Upstream from the TATA box, putative control elements corresponding to the concensus sequences for the RPG box and the general amino acid control system were identified. Evidence for transcriptional induction of the KRS1 gene via the general amino acid control system is presented.
Highlights
The nucleotide sequence of 3a.6-kilobase pair DNA structural domain of M, -8,000 carrying a cationic net charge fragment containing the structural gene for yeascty- responsible for association with polyanionic carriers
The location of the KRSl gene, correspondingto yeast lysyltRNA synthetase, was determined by the characterizationof twootherrecombinant clones, one of themallowing the by size exclusion chromatography, and subcloned in suitable nondephosphorylated M13mp18or M13mp19 DNA whichwas made free of its excised polylinker fragment
By using It was previously shown that the aptitude of the native a 600-nucleotide-long anti-RNA probe corresponding to the lysyl-tRNA synthetase to interact with polyanionic carriers internal EcoRI-EcoRI fragment of the KRSl gene, a unique in uitro was strongly decreased on elastase conversion to a polyadenylated mRNA of 1900-2000 nucleotides was detected fully active modified dimer of subunit M, 67,000 and was by Northern blot analysis (Fig. 3)
Summary
This articlemust be hereby marked “advertisement” in Materials-Restriction endonucleases and DNA-modifying enaccordance with 18U.S.C.
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