Contribution of arginase to manganese metabolism of Aspergillus niger
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Aspects of manganese metabolism during normal and acidogenic growth of Aspergillus niger were explored. Arginase from this fungus was a Mn[II]-enzyme. The contribution of the arginase protein towards A. niger manganese metabolism was investigated using arginase knockout (D-42) and arginase over-expressing (ΔXCA-29) strains of A. niger NCIM 565. The Mn[II] contents of various mycelial fractions were found in the order: D-42 strain < parent strain < ΔXCA-29 strain. While the soluble fraction forms 60 % of the total mycelial Mn[II] content, arginase accounted for a significant fraction of this soluble Mn[II] pool. Changes in the arginase levels affected the absolute mycelial Mn[II] content but not its distribution in the various mycelial fractions. The A. niger mycelia harvested from acidogenic growth media contain substantially less Mn[II] as compared to those from normal growth media. Nevertheless, acidogenic mycelia harbor considerable Mn[II] levels and a functional arginase. Altered levels of mycelial arginase protein did not significantly influence citric acid production. The relevance of arginase to cellular Mn[II] pool and homeostasis was evaluated and the results suggest that arginase regulation could occur via manganese availability.
KeywordsAspergillus niger Arginase Manganese metabolism Acidogenic growth
We acknowledge Sophisticated Analysis and Instrumentation Facility (SAIF), Department of Earth Sciences, and Centre for Environmental Science and Engineering (CESE) at IIT Bombay for support in Mn[II] analyses. Dr. Neetu Singh performed early standardizations of A. niger growth inhibition by Mn[II]. The work was supported by a grant from Board of Research in Nuclear Sciences (BRNS), Department of Atomic Energy (DAE) and fellowship (to Sarita Keni) by Council of Scientific and Industrial Research (CSIR).
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Conflict of interest
The authors declare that they have no conflict of interest.
- Auling G (1994) Manganese: function and transport in fungi. In: Winkelmann G, Winge DR (eds) Metal ions in fungi. Marcel Dekker, New York, pp 215–236Google Scholar
- Crowley JD, Traynor DA, Weatherburn DC (2000) Enzymes and proteins containing manganese: An overview. In: Sigel A, Sigel H (eds) Metal ions in biological systems. Marcel Dekker, New York, pp 209–277Google Scholar
- Davis RH, Weiss RL, Bowman BJ (1978) Intracellular metabolite distribution as a factor in regulation in Neurospora. In: Microenvironments and metabolic compartmentation. Academic Press, New York, pp 197–207Google Scholar
- Hockertz S, Schmid J, Auling G (1987) A specific transport system for manganese in the filamentous fungus Aspergillus niger. J Gen Microbiol 133:3513–3519Google Scholar
- Jayashri TN, Anuradha R, Punekar NS (2009) Single-stranded megaprimer splicing through OE-PCR: construction of full-length Aspergillus niger arginase cDNA. Ind J Biochem Biophys 46:266–268Google Scholar
- Komachi Y, Hatakeyama S, Motomatsu H, Futagami T, Kizjakina K, Sobrado P, Ekino K, Takegawa K, Goto M, Nomura Y, Oka T (2013) gfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Mol Microbiol 90:1054–1073CrossRefPubMedCentralPubMedGoogle Scholar
- Kosman DJ (1994) Transition metal ion uptake in yeasts and filamentous fungi. In: Winkelmann G, Winge DR (eds) Metal ions in fungi. Marcel Dekker, New York, pp 1–38Google Scholar
- Lopez V, Alarcon R, Orellana MS, Enriquez P, Uribe E, Martinez J, Carvajal N (2005) Insights into the interaction of human arginase II with substrate and manganese ions by site-directed mutagenesis and kinetic studies. Alteration of substrate specificity by replacement of Asn149 with Asp. FEBS J 272:4540–4548CrossRefPubMedGoogle Scholar
- McNaughton RL, Reddi AR, Clement MH, Sharma A, Barnese K, Rosenfeld L, Gralla EB, Valentine JS, Culotta VC, Hoffman BM (2010) Probing in vivo Mn2+ speciation and oxidative stress resistance in yeast cells with electron-nuclear double resonance spectroscopy. Proc Natl Acad Sci USA 107:15335–15339CrossRefPubMedCentralPubMedGoogle Scholar
- Pinchai N, Juvvadi PR, Fortwendel JR, Perfect BZ, Rogg LE, Asfaw YG, Steinbach WJ (2010) The Aspergillus fumigatus P-type Golgi apparatus Ca2+/Mn2+ ATPase PmrA is involved in cation homeostasis and cell wall integrity but is not essential for pathogenesis. Eukaryot Cell 9:472–476CrossRefPubMedCentralPubMedGoogle Scholar