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Molecular machines encoded by bacterially‐derived multi‐domain gene fusions that potentially synthesize, N ‐methylate and transfer long chain polyamines in diatoms
Author(s) -
Michael Anthony J.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.07.038
Subject(s) - polyamine , biochemistry , methyltransferase , biology , horizontal gene transfer , gene , biosynthesis , enzyme , chemistry , methylation , genome
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.