Prokaryotic origin of cytidylyltransferases and α-ketoacid synthases

α-Ketoacids are present in glycosylated structures in almost all organisms and must be activated by a cytidylyltransferase (CT) before their incorporation into glycoconjugates. Examples of α-ketoacids include KDO (keto-deoxyoctulosonic acid), which is present in bacterial lipopolysaccharide and in p...

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Veröffentlicht in:Trends in microbiology (Regular ed.) 2004-03, Vol.12 (3), p.120-128
Hauptverfasser: Bravo, Ignacio G., Garcı́a-Vallvé, Santiago, Romeu, Antoni, Reglero, Ángel
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Sprache:eng
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Zusammenfassung:α-Ketoacids are present in glycosylated structures in almost all organisms and must be activated by a cytidylyltransferase (CT) before their incorporation into glycoconjugates. Examples of α-ketoacids include KDO (keto-deoxyoctulosonic acid), which is present in bacterial lipopolysaccharide and in plant pectins, and sialic acids (Sia), such as N-acetylneuraminate (NeuAc), which are present in animals and in pathogenic microorganisms. The phylogeny of Sia and CTs is unclear but is linked to the history of the α-ketoacid synthases. Furthermore, horizontal gene transfer (HGT) events might have played a major role. Here we analyse the origin and the expansion process of these genes with respect to the taxonomic coherence of the phylogenetic trees, the molecular characteristics of the CT-coding DNA and the presence or absence of a long C-terminal coding region in some NeuAc-CTs. We propose a prokaryotic origin for CTs and α-ketoacid synthases, and a HGT event of these genes towards ancestors of animals and plants. Finally, some pathogenic bacteria reacquired some of these genes, which would have been modified and devoted to Sia synthesis.
ISSN:0966-842X
1878-4380
DOI:10.1016/j.tim.2004.01.004