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VOL. 7: 281-285 (1991)
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Complete Sequence of the Saccharomyces cerevisiae LE U l Gene Encoding Isopropylmalate Isomerase JACEK SKALA, ETIENNE CAPIEAUX, ELISABETTA BALZI, WEINING CHEN AND ANDRE GOFFEAU* Unite' de Biochimie Physiologique, Universite'Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium *Institute of Microbiology, Wroclaw University, Przybyszewskiego 63,51-148 Wroclaw,Poland
Received 28 July 1990; revised 6 November 1990 We have sequenced the Saccharomyces cerevisiae (strain IL125-2B) LEU1 gene which encodes isopropylmalate isomerase (EC 4.2.1.33) the second enzyme specific for leucine biosynthesis (Gross et al., 1962, 1963). The LEU1 gene is located between the PMAI (Serrano et al., 1986; Ulaszewski et al., 1987) and scll (Balzi et al., 1989) genes (for a map see Capieaux et al., 1991), about 5.2 cM from the centromere on the left arm of chromosome VII (Ulaszewski et a/., 1987). The LEU1 gene was cloned by gene complementation as previously described (Balzi et al.,1987; Ulaszewski et al., 1987). The leu1 mutation is complemented by integration of a DNA fragment which contains the complete promotor together with 153 nucleotides from the 5' end of the LEUl coding region (Ulaszewski et al., 1987). The nucleotide sequence of LEUl is contiguous at the 5' end to the sequences published by Hsu and Schimmel(l984) and Capieaux et al. (1989). It is also contiguous at the 3' end to the sequence published by Balzi et al. (1989) and Chen et al. (1991).
THE OPEN READING FRAME The protein predicted from the nucleotide sequence comprises 782 amino acids (Figure 1) and has a molecular weight of 86.1 kDa, in close agreement with the molecular weight of 90 kDa determined for the purifed yeast isopropylmalate isomerase (Bigelis and Umbarger, 1976). Northern analysis revealed a polyadenylated LEUl mRNA of 2.7 kb (Capieaux et *Corresponding author.
0749-503)
VOL. 7: 281-285 (1991)
0 0 0 0
0
:VII :Yeast Sequencing Reports 0 0 0 0
Complete Sequence of the Saccharomyces cerevisiae LE U l Gene Encoding Isopropylmalate Isomerase JACEK SKALA, ETIENNE CAPIEAUX, ELISABETTA BALZI, WEINING CHEN AND ANDRE GOFFEAU* Unite' de Biochimie Physiologique, Universite'Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium *Institute of Microbiology, Wroclaw University, Przybyszewskiego 63,51-148 Wroclaw,Poland
Received 28 July 1990; revised 6 November 1990 We have sequenced the Saccharomyces cerevisiae (strain IL125-2B) LEU1 gene which encodes isopropylmalate isomerase (EC 4.2.1.33) the second enzyme specific for leucine biosynthesis (Gross et al., 1962, 1963). The LEU1 gene is located between the PMAI (Serrano et al., 1986; Ulaszewski et al., 1987) and scll (Balzi et al., 1989) genes (for a map see Capieaux et al., 1991), about 5.2 cM from the centromere on the left arm of chromosome VII (Ulaszewski et a/., 1987). The LEU1 gene was cloned by gene complementation as previously described (Balzi et al.,1987; Ulaszewski et al., 1987). The leu1 mutation is complemented by integration of a DNA fragment which contains the complete promotor together with 153 nucleotides from the 5' end of the LEUl coding region (Ulaszewski et al., 1987). The nucleotide sequence of LEUl is contiguous at the 5' end to the sequences published by Hsu and Schimmel(l984) and Capieaux et al. (1989). It is also contiguous at the 3' end to the sequence published by Balzi et al. (1989) and Chen et al. (1991).
THE OPEN READING FRAME The protein predicted from the nucleotide sequence comprises 782 amino acids (Figure 1) and has a molecular weight of 86.1 kDa, in close agreement with the molecular weight of 90 kDa determined for the purifed yeast isopropylmalate isomerase (Bigelis and Umbarger, 1976). Northern analysis revealed a polyadenylated LEUl mRNA of 2.7 kb (Capieaux et *Corresponding author.
0749-503)
