Journal Article

Differential roles of pyruvate decarboxylase in aerial and embedded mycelia of the ascomycete <i>Gibberella zeae</i>

Hokyoung Son, Kyunghun Min, Jungkwan Lee, Gyung Ja Choi, Jin-Cheol Kim and Yin-Won Lee

in FEMS Microbiology Letters

Volume 329, issue 2, pages 123-130
Published in print April 2012 |
Published online March 2012 | e-ISSN: 1574-6968 | DOI: http://dx.doi.org/10.1111/j.1574-6968.2012.02511.x

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Abstract

The pyruvate–acetaldehyde–acetate (PAA) pathway has diverse roles in eukaryotes. Our previous study on acetyl-coenzyme A synthetase 1 (ACS1) in Gibberella zeae suggested that the PAA pathway is important for lipid production, which is required for perithecia maturation. In this study, we deleted all three pyruvate decarboxylase (PDC) genes, which encode enzymes that function upstream of ACS1 in the PAA pathway. Results suggest PDC1 is required for lipid accumulation in the aerial mycelia, and deletion of PDC1 resulted in highly wettable mycelia. However, the total amount of lipids in the PDC1 deletion mutants was similar to that of the wild-type strain, likely due to compensatory lipid production processes in the embedded mycelia. PDC1 was expressed both in the aerial and embedded mycelia, whereas ACS1 was observed only in the aerial mycelia in a PDC1-dependent manner. PDC1 is also involved in vegetative growth of embedded mycelia in G. zeae, possibly through initiating the ethanol fermentation pathway. Thus, PDC1 may function as a key metabolic enzyme crucial for lipid production in the aerial mycelia, but play a different role in the embedded mycelia, where it might be involved in energy generation by ethanol fermentation.

Keywords: Fusarium graminearum; pyruvate decarboxylase; triacylglyceride

Journal Article.  3949 words.  Illustrated.

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