Journal
FEBS LETTERS
Volume 585, Issue 17, Pages 2627-2634Publisher
WILEY
DOI: 10.1016/j.febslet.2011.07.038
Keywords
Diatom; Biosilica glass; Long chain polyamine biosynthesis; N-methylation; Aminopropyltransferase
Funding
- University of Texas Southwestern Medical Center
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Silica glass formation in diatoms requires the biosynthesis of unusual, very long chain polyamines (LCPA) composed of iterated aminopropyl units. Diatoms processively synthesize LCPA, N-methylate the amine groups and transfer concatenated, N-dimethylated aminopropyl groups to silaffin proteins. Here I show that diatom genomes possess signal peptide-containing gene fusions of bacterially-derived polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC) and an aminopropyltransferase, sometimes fused to a eukaryotic histone N-methyltransferase domain, that potentially synthesize and N-methylate LCPA. Fusions of similar, alternatively configured domains but with a catalytically dead AdoMetDC and in one case a Tudor domain, may N-dimethylate and transfer multiple aminopropyl unit polyamines onto silaffin proteins. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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