The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes

Andreas F. Glas, Melanie J. Maul, Max Cryle, Thomas R M Barends, Sabine Schneider, Emine Kaya, Ilme Schlichting, Thomas Carell

Research output: Contribution to journalArticleResearchpeer-review

48 Citations (Scopus)

Abstract

Archae possess unique biochemical systems quite distinct from the pathways present in eukaryotes and eubacteria. 7,8-Dimethyl-8-hydroxy-5deazaflavin (F0) and F420 are unique deazaflavin-containing coenzyme and methanogenic signature molecules, essential for a variety of biochemical transformations associated with methane biosynthesis and light-dependent DNA repair. The deazaflavin cofactor system functions during methane biosynthesis as a low-potential hydrid shuttle F420/F420H2. In DNA photolyase repair proteins, the deazaflavin cofactor is in the deprotonated state active as a light-collecting energy transfer pigment. As such, it converts blue sunlight into energy used by the proteins to drive an essential repair process. Analysis of a eukaryotic (6-4) DNA photolyase from Drosophila melanogaster revealed a binding pocket, which tightly binds F0. Residues in the pocket activate the cofactor by deprotonation so that light absorption and energy transfer are switched on. The crystal structure of F 0 in complex with the D. melanogaster protein shows the atomic details of F0 binding and activation, allowing characterization of the residues involved in F0 activation. The results show that the F0/F420 coenzyme system, so far believed to be strictly limited to the archael kingdom of life, is far more widespread than anticipated. Analysis of a D. melanogaster extract and of a DNA photolyase from the primitive eukaryote Ostreococcus tauri provided direct proof for the presence of the F0 cofactor also in higher eukaryotes.

Original languageEnglish
Pages (from-to)11540-11545
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number28
DOIs
Publication statusPublished - 14 Jul 2009
Externally publishedYes

Keywords

  • Crystal structure
  • Deazaflavin
  • DNA photolesion
  • DNA repair
  • Photolyase

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