Author
 |
LAL, SHAILESH - UNIV OF ILLINOIS, URBANA |
|
Sachs, Martin |
|
Submitted to: Plant Physiology Plant Gene Register Electronic Submission
Publication Type: Other Publication Acceptance Date: 12/21/1994 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Glucose-6 phosphate isomerase (GPI; EC 5.3.1.9) is an essential glycolytic enzyme that catalyzes the reversible isomerization of Glucose-6-phosphate and Fructose-6-phosphate. The enzymatic activity of GPI has been reported to be induced under anaerobic stress in maize (Kelley and Freeling 1984). Using electrophoretically distinguishable alleles of GPI and antibodies against spinach cytosolic GPI, Kelley and Freeling (1984) identified ANP55 in maize as an isozyme of GPI-C encoded by the phi1 gene. To analyze the source of the multiple GPI isozymes and to study their anaerobic regulation, we isolated 25 clones from a cDNA library constructed from maize roots treated anaerobically for 6 hours. The GPI clones were isolated using a heterologous cDNA probe encoding GPI-C from Arabidopsis (generously provided by Les Gottieb; Thomas et al., 1993). The clone with the longest insert (2.1 kb) had an open reading frame encoding a protein of 567 amino acid residues with high sequence identity to GPI sequences from other species. Northern blot analysis using the full length cDNA probe detected a dramatic induction of transcript levels in maize roots upon anaerobic treatment. Using this cDNA as a probe in RFLP mapping showed that its gene is located on maize chromosome 1L, within a couple of map units of where the phi1 gene is expected to be localized, strongly indicating that the GPI cDNA is encoded by this gene (Ed Coe et al., personal communication). |
