Journal Article

FZJ-2020-03140

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Complex evolution of light-dependent protochlorophyllide oxidoreductases in aerobic anoxygenic phototrophs: origin, phylogeny and function

Chernomor, O. ; Peters, L. ; Schneidewind, J. ; Loeschcke, A.FZJ* ; Knieps-Grünhagen, E.FZJ* ; Schmitz, F. ; von Lieres, E.FZJ* ; Kutta, R. J. ; Svensson, V. ; Jaeger, K.-E.FZJ* ; Drepper, T.FZJ* ; von Haeseler, A. ; Krauss, U. (Corresponding author)FZJ*

2021
Oxford Univ. Press Oxford

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Please use a persistent id in citations: http://hdl.handle.net/2128/30063  doi:10.1093/molbev/msaa234

Abstract: Light-dependent and dark-operative protochlorophyllide oxidoreductases (LPORs and DPORs) are evolutionary and structurally distinct enzymes that are essential for the synthesis of (bacterio)chlorophyll, the primary pigment needed for both anoxygenic and oxygenic photosynthesis. In contrast to the long-held hypothesis that LPORs are only present in oxygenic phototrophs, we recently identified a functional LPOR in the aerobic anoxygenic phototrophic bacterium (AAPB) Dinoroseobacter shibae, and attributed its presence to a single horizontal gene transfer (HGT) event from cyanobacteria. Here, we provide evidence for the more widespread presence of genuine LPOR enzymes in AAPBs. An exhaustive bioinformatics search identified 36 putative LPORs outside of oxygenic phototrophic bacteria (cyanobacteria) with the majority being AAPBs. Using in vitro and in vivo assays, we show that the large majority of the tested AAPB enzymes are genuine LPORs. Solution structural analyses, performed for two of the AAPB LPORs, revealed a globally conserved structure when compared to a well-characterized cyanobacterial LPOR. Phylogenetic analyses suggest that LPORs were transferred not only from cyanobacteria, but also subsequently between proteobacteria and from proteobacteria to Gemmatimonadetes. Our study thus provides another interesting example for the complex evolutionary processes that govern the evolution of bacteria, involving multiple HGT events that likely occurred at different time points and involved different donors.

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Contributing Institute(s):

1. Biotechnologie (IBG-1)
2. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)

Research Program(s):

1. 2171 - Biological and environmental resources for sustainable use (POF4-217) (POF4-217)

Appears in the scientific report 2021

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