A slow growing inl+/- mutant was isolated from an inositol dependent (inl) Neurospora crassa strain. The latter strain produces defective myo-inositol-1-phosphate synthase which has residual activity. Inositol, similarly to that found in wild and inl mutant strains, represses the enzyme production in the inl+/- strain as well. Withdrawing inositol from the medium results in derepression of the enzyme synthesis. Derepression is hindered by cycloheximide. Inl+/- character in the double mutant is brought about by overproduction of the defective myo-inositol-1-phosphate synthase.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Plants distinguish different photoperiods to independently control seasonal flowering and growth.
Science
February 2024
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA.
Plants measure daylength (photoperiod) to regulate seasonal growth and flowering. Photoperiodic flowering has been well studied, but less is known about photoperiodic growth. By using a mutant with defects in photoperiodic growth, we identified a seasonal growth regulation pathway that functions in long days in parallel to the canonical long-day photoperiod flowering mechanism.
View Article and Find Full Text PDFDisruption of , a Gene Encoding -Inositol Phosphate Synthase, Causes Male Sterility in .
G3 (Bethesda)
August 2018
Department of Biological Sciences, California State University Long Beach, Long Beach, California
Inositol is a precursor for the phospholipid membrane component phosphatidylinositol (PI), involved in signal transduction pathways, endoplasmic reticulum stress, and osmoregulation. Alterations of inositol metabolism have been implicated in human reproductive issues, the therapeutic effects of drugs used to treat epilepsy and bipolar disorder, spinal cord defects, and diseases including diabetes and Alzheimer's. The sole known inositol synthetic enzyme is -inositol synthase (MIPS), and the homolog in is encoded by the gene.
View Article and Find Full Text PDFCharacterization of the inositol monophosphatase gene family in Arabidopsis.
Front Plant Sci
January 2015
Department of Biochemistry, Virginia Polytechnic Institute and State University Blacksburg, VA, USA.
Synthesis of myo-inositol is crucial in multicellular eukaryotes for production of phosphatidylinositol and inositol phosphate signaling molecules. The myo-inositol monophosphatase (IMP) enzyme is required for the synthesis of myo-inositol, breakdown of inositol (1,4,5)-trisphosphate, a second messenger involved in Ca(2+) signaling, and synthesis of L-galactose, a precursor of ascorbic acid. Two myo-inositol monophosphatase -like (IMPL) genes in Arabidopsis encode chloroplast proteins with homology to the prokaryotic IMPs and one of these, IMPL2, can complement a bacterial histidinol 1-phosphate phosphatase mutant defective in histidine synthesis, indicating an important role for IMPL2 in amino acid synthesis.
View Article and Find Full Text PDFGlutamate and lipid metabolic perturbation in the hippocampi of asymptomatic borna disease virus-infected horses.
PLoS One
October 2015
Department of Neurology, The First Affiliated Hospital of Chongqing Medical University, Chongqing, China; Institute of Neuroscience, Chongqing Medical University, Chongqing, China; Chongqing Key Laboratory of Neurobiology, Chongqing Medical University, Chongqing, China.
Borna disease virus (BDV) is a neurotropic, enveloped, non-segmented, negative-stranded RNA virus that infects a wide variety of vertebrate species from birds to humans across a broad global geographic distribution. Animal symptomatology range from asymptomatic infection to behavioral abnormalities to acute meningoencephalitis. Asymptomatic BDV infection has been shown to be more frequent than conventionally estimated.
View Article and Find Full Text PDFRegulation of inositol metabolism is fine-tuned by inositol pyrophosphates in Saccharomyces cerevisiae.
J Biol Chem
August 2013
Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202, USA.
Although inositol pyrophosphates have diverse roles in phosphate signaling and other important cellular processes, little is known about their functions in the biosynthesis of inositol and phospholipids. Here, we show that KCS1, which encodes an inositol pyrophosphate kinase, is a regulator of inositol metabolism. Deletion of KCS1, which blocks synthesis of inositol pyrophosphates on the 5-hydroxyl of the inositol ring, causes inositol auxotrophy and decreased intracellular inositol and phosphatidylinositol.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!