Iron-sulfur proteins in anaerobic eukaryotes

Cammack, Richard, Horner, David S., van der Giezen, Mark, Kulda, Jaroslav and Lloyd, David ORCID: https://orcid.org/0000-0002-5656-0571 2007. Iron-sulfur proteins in anaerobic eukaryotes. Ljungdahl, Lars G., Adams, Michael W., Barton, Larry L., Ferry, James G. and Johnson, Michael K., eds. Biochemistry and Physiology of Anaerobic Bacteria, New York, NY: Springer, pp. 113-127. (10.1007/0-387-22731-8_9)

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Abstract

The phylogeny and unexpected distribution of hydrogenase-related genes among extant organisms suggest an ancient and crucial role for members of this gene family in eukaryotes and are consistent with hydrogen syntrophy based models of eukaryogenesis. For the protists studied, the available data are consistent with a mitochondrial origin for the hydrogenosomes. But one needs to realize that the origin of the enzymes need not necessarily be the same as the origin of the organellar structure. The hydrogenosomes may have originated several times in the course of evolution, with lateral transfer of genes from other eukaryotes or anaerobic bacteria. At present, the lack of a well-supported sister group to the eukaryotes prevents discrimination between the ideas presented in the hydrogen and syntrophic hypotheses. Furthermore, the most parsimonious explanation of these observations is that many eukaryotes, such as the green algae, retained ancestral energy metabolic genes that were available for recruitment during adaptation to anaerobic and, in at least one case, photosynthetic lifestyles, a remarkable demonstration of the plasticity of eukaryote molecular physiology.

Item Type:	Book Section
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Springer
ISBN:	978-0-387-95592-6
Last Modified:	26 Oct 2022 08:32
URI:	https://orca.cardiff.ac.uk/id/eprint/127731

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