Literature DB >> 24566086

Analysis of covalent flavinylation using thermostable succinate dehydrogenase from Thermus thermophilus and Sulfolobus tokodaii lacking SdhE homologs.

Asako Kounosu1.   

Abstract

Recent studies have indicated that post-translational flavinylation of succinate dehydrogenase subunit A (SdhA) in eukaryotes and bacteria require the chaperone-like proteins Sdh5 and SdhE, respectively. How does covalent flavinylation occur in prokaryotes, which lack SdhE homologs? In this study, I showed that covalent flavinylation in two hyperthermophilic bacteria/archaea lacking SdhE, Thermus thermophilus and Sulfolobus tokodaii, requires heat and dicarboxylic acid. These thermophilic bacteria/archaea inhabit hot environments and are said to be genetically far removed from mesophilic bacteria which possess SdhE. Since mesophilic bacteria have been effective at covalent bonding in temperate environments, they may have caused the evolution of SdhE.
Copyright © 2014 The Author. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Covalent flavinylation; SDH subunit A; Sdh5; Succinate dehydrogenase protein E; Sulfolobus tokodaii; Thermus thermophilus

Mesh:

Substances:

Year:  2014        PMID: 24566086     DOI: 10.1016/j.febslet.2014.02.022

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  11 in total

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6.  The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.

Authors:  Pankaj Sharma; Elena Maklashina; Gary Cecchini; T M Iverson
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Review 7.  Protein-mediated assembly of succinate dehydrogenase and its cofactors.

Authors:  Jonathan G Van Vranken; Un Na; Dennis R Winge; Jared Rutter
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8.  Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.

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Journal:  J Biol Chem       Date:  2015-12-07       Impact factor: 5.157

9.  Crystal structure of an assembly intermediate of respiratory Complex II.

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Journal:  Biomolecules       Date:  2020-04-10
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