Expansion of the redox-sensitive proteome coincides with the plastid endosymbiosis

Nature Plants
Christian WoehleShilo Rosenwasser

Abstract

The redox-sensitive proteome (RSP) consists of protein thiols that undergo redox reactions, playing an important role in coordinating cellular processes. Here, we applied a large-scale phylogenomic reconstruction approach in the model diatom Phaeodactylum tricornutum to map the evolutionary origins of the eukaryotic RSP. The majority of P. tricornutum redox-sensitive cysteines (76%) is specific to eukaryotes, yet these are encoded in genes that are mostly of a prokaryotic origin (57%). Furthermore, we find a threefold enrichment in redox-sensitive cysteines in genes that were gained by endosymbiotic gene transfer during the primary plastid acquisition. The secondary endosymbiosis event coincides with frequent introduction of reactive cysteines into existing proteins. While the plastid acquisition imposed an increase in the production of reactive oxygen species, our results suggest that it was accompanied by significant expansion of the RSP, providing redox regulatory networks the ability to cope with fluctuating environmental conditions.

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Citations

May 16, 2017·Nature Plants·William F Martin, Helmut Sies
May 2, 2018·The Journal of Experimental Biology·Paulo CartaxanaSónia Cruz
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Apr 14, 2021·Current Biology : CB·Duckhyun LheeHwan Su Yoon
Sep 28, 2021·Frontiers in Microbiology·Shiri Graff van CreveldAssaf Vardi
Oct 8, 2021·Free Radical Biology & Medicine·Shani DoronShilo Rosenwasser

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Software Mentioned

Ontologizer
BLASTP
PSIBLAST
MAFFT
PAML
EMBOSS
UNCys

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