Nucleotide sequencing analysis of a LEU gene of Candida maltosa which complements leuB mutation of Escherichia coli and leu2 mutation of Saccharomyces cerevisiae

Takagi, Masamichi; Kobayashi, Norio; Sugimoto, Masanori; Fujii, Toshio; Watari, Junji; Yano, Keiji

doi:10.1007/bf00384606

Cited by 36 publications

(24 citation statements)

References 25 publications

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“…When dehydrogenase was missing, synthase activity again increased 4-to 6-fold while isomerase activity rose 12-to 20-fold. These data are not easily interpreted in terms of known regulatory mechanisms and appear to be at odds with an earlier report that a cloned gene from C. maltosa that showed 76% homology (at the protein sequence level) to LEU2 from S. cerevisiae (4), and was therefore named C-LEU2, was regulated just like LEU2 from S. cerevisiae when transferred into that organism (100). The interpretation of genetic data from C. maltosa is complicated by evidence of a highly aneuploid genome and the spontaneous occurrence of auxotrophy-prototrophy-auxotrophy changes due to the presence of silent gene copies (8).…”

Section: Other Speciescontrasting

confidence: 79%

Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door

Kohlhaw

2003

Microbiol Mol Biol Rev

213

249

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After exploring evolutionary aspects of branched-chain amino acid biosynthesis, the review focuses on the extended leucine biosynthetic pathway as it operates in Saccharomyces cerevisiae. First, the genes and enzymes specific for the leucine pathway are considered: LEU4 and LEU9 (encoding the α-isopropylmalate synthase isoenzymes), LEU1 (isopropylmalate isomerase), and LEU2 (β-isopropylmalate dehydrogenase). Emphasis is given to the unusual distribution of the branched-chain amino acid pathway enzymes between mitochondrial matrix and cytosol, on the newly defined role of Leu5p, and on regulatory mechanisms governing gene expression and enzyme activity, including new evidence for the metabolic importance of the regulation of α-isopropylmalate synthase by coenzyme A. Next, structure-function relationships of the transcriptional regulator Leu3p are addressed, defining its dual role as activator and repressor and discussing evidence in support of the self-masking model. Recent data pointing at a more extended Leu3p regulon are discussed. An overview of the layered controls of the extended leucine pathway is provided that includes a description of the newly recognized roles of Ilv5p and Bat1p in maintaining mitochondrial integrity. Finally, branched-chain amino acid biosynthesis and its regulation in other fungi are summarized, the question of leucine as metabolic signal is addressed, and possible directions of future research in this area are outlined

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Section: Other Speciescontrasting

confidence: 79%

Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door

Kohlhaw

2003

Microbiol Mol Biol Rev

213

249

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“…The gene sequence showed good homology to the nifS genes in the nitrogen-fixing bacteria Azotobacter vinelandii and A. chroococcum, Anabaena sp., and Kiebsiella pneumoniae (31). A data base search also showed that the dimorphic yeast Candida maltosa contained a highly homologous gene located at the same chromosomal position as nfsl, i.e., adjacent to LEU2 (31,44).…”

Section: Resultsmentioning

confidence: 97%

“…The references for the sequences are (GenBank/EMBL accession no.) as follows: C. mal, C. maltosa (44), X05459; S. cer, S. cerevisiae (31), Swissprot no. P25374 and GenBank no.…”

Section: Resultsmentioning

confidence: 99%

SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing

Kolman

Söll

1993

J Bacteriol

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A genetic approach was used to isolate and characterize Saccharomyces cerevisiae genes affecting tRNA processing. Three mutants were isolated which were able to process and utilize splicing-deficient transcripts from inactivated Schizosaccharomyces pombe suppressor tRNA genes. Extragenic recovery of suppressibility was verified by the suppression of nonsense mutations in LEU2, HIS4, and ADE1. One mutant, SPL1-1, was chosen for detailed analysis on the basis of its increased synthesis of mature suppressor tRNA over wild-type cell levels as determined by Northern (RNA) analysis. This mutant exhibited strong suppression exclusively with the defective tRNA gene used in the mutant selection. Genetic analysis revealed that a single, dominant, haplo-lethal mutation was responsible for the suppression phenotype. The mutation mapped on chromosome III to an essential 1.5-kb open reading frame (L. S. Symington and T. D. Petes, Mol. Cell. Biol. 8:595-604, 1988), recently named NFS1 (S. G. Oliver et al., Nature [London] 357:38-46, 1992), located adjacent (centromere proximal) to LEU2.

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“…This enzyme is on the leucine biosynthetic pathway. The leuB gene encoding IPMDH has been cloned and sequenced from a variety of microorganisms such as yeasts (2,6,7,26,34), bacilli (11,29,30). Salmonella typhimurium (3), a cyanobacterium, Spirulina platensis (4), and two extreme thermophiles, Thermus thermophilus (12,14) and Thermus aquaticus (15).…”

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confidence: 99%

Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method

et al. 1996

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We succeeded in further improvement of the stability of 3-isopropylmalate dehydrogenase (IPMDH) from an extreme thermophile, Thermus thermophilus, by a suppressor mutation method. We previously constructed a chimeric IPMDH consisting of portions of thermophile and mesophile enzymes. The chimeric enzyme is less thermostable than the thermophile enzyme. The gene encoding the chimeric enzyme was subjected to random mutagenesis and integrated into the genome of a leuB-deficient mutant of T. thermophilus. The transformants were screened at 76؇C in minimum medium, and three independent stabilized mutants were obtained. The leuB genes from these three mutants were cloned and analyzed. The sequence analyses revealed Ala-1723Val substitution in all of the mutants. The thermal stability of the thermophile IPMDH was improved by introducing the amino acid substitution.

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Nucleotide sequencing analysis of a LEU gene of Candida maltosa which complements leuB mutation of Escherichia coli and leu2 mutation of Saccharomyces cerevisiae

Cited by 36 publications

References 25 publications

Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door

Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door

SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing

Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method

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