Note. The novel nucleotide sequence data published here have been submitted to the EMBL sequence data bank and are available under accession number X61271.
The ICL1 gene from Saccharomyces cerevisiae
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 204, Issue 3, pages 983–990, March 1992
How to Cite
FERNÁNDEZ, E., MORENO, F. and RODICIO, R. (1992), The ICL1 gene from Saccharomyces cerevisiae. European Journal of Biochemistry, 204: 983–990. doi: 10.1111/j.1432-1033.1992.tb16720.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received August 2, 1991) – EJB 91 1039
The glyoxylate cycle is essential for the utilization of C2 compounds by the yeast Saccharomyces cerevisiae. Within this cycle, isocitrate lyase catalyzes one of the key reactions. We obtained mutants lacking detectable isocitrate lyase activity, screening for their inability to grow on ethanol. Genetic and biochemical analysis suggested that they carried a defect in the structural gene, ICL1. The mutants were used for the isolation of this gene and it was located on a 3.1-kb Bg/II-SphI DNA fragment. We then constructed a deletion-substitution mutant in the haploid yeast genome. It did not have any isocitrate lyase activity and lacked the ability to grow on ethanol as the sole carbon source. Both strands of a DNA fragment carrying the gene and its flanking regions were sequenced. An open reading frame of 1671 bp was detected, encoding a protein of 557 amino acids with a calculated molecular mass of 62515 Da. The deduced amino acid sequence shows extensive similarities to genes encoding isocitrate lyases from various organisms. Two putative cAMP-dependent protein-kinase phosphorylation sites may explain the susceptibility of the enzyme to carbon catabolite inactivation.