Principal component analysis of the codon-usage of the hydrogenase and mitochondrial 24/51 kDa modules

Copyright information:Taken from "The [FeFe] hydrogenase of has a chimeric origin"http://www.biomedcentral.com/1471-2148/7/230BMC Evolutionary Biology 2007;7():230-230.Published online 16 Nov 2007PMCID:PMC2216082. While most of the strains exhibit only slight differences in codon-preferenc...

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Hauptverfasser: Boxma, Brigitte, Guénola Ricard, Hoek, Angela HAM Van, Severing, Edouard, Seung-Yeo Moon-Van Der Staay, Staay, Georg WM Van Der, Alen, Theo A Van, Graaf, Rob M De, Cremers, Geert, Kwantes, Michiel, McEwan, Neil R, C Jamie Newbold, Jouany, Jean-Pierre, Michalowski, Tadeusz, Pristas, Peter, Huynen, Martijn A, Hackstein, Johannes HP
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Sprache:eng
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Zusammenfassung:Copyright information:Taken from "The [FeFe] hydrogenase of has a chimeric origin"http://www.biomedcentral.com/1471-2148/7/230BMC Evolutionary Biology 2007;7():230-230.Published online 16 Nov 2007PMCID:PMC2216082. While most of the strains exhibit only slight differences in codon-preference, the isolate from the host cockroach strain Amsterdam has a substantially different codon-usage. In both cases, the bacterial-derived 24 and 51 kDa modules acquired the typical ciliate codon-usage that is not significantly different from the one used for the (nuclear-encoded) mitochondrial modules. Even the top-down distribution shows a complete ameliorisation of the modules.
DOI:10.6084/m9.figshare.69896