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Hybrid cluster proteins in a photosynthetic microalga
Author(s) -
Lis Robert,
Brugière Sabine,
Baffert Carole,
Couté Yohann,
Nitschke Wolfgang,
Atteia Ariane
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15025
Subject(s) - chlamydomonas reinhardtii , photosynthesis , gene cluster , gene , thermophile , biology , phylogenetic tree , bacteria , chemistry , biochemistry , genetics , mutant
Hybrid cluster proteins (HCPs) are metalloproteins characterized by the presence of an iron‐sulfur‐oxygen cluster. These proteins occur in all three domains of life. In eukaryotes, HCP s have so far been found only in a few anaerobic parasites and photosynthetic microalgae. With respect to all species harboring an HCP , the green microalga Chlamydomonas reinhardtii stands out by the presence of four HCP genes. The study of the gene and protein structures as well as the phylogenetic analyses strongly support a model in which the HCP family in the alga has emerged from a single gene of alpha proteobacterial origin and then expanded by several rounds of duplications. The spectra and redox properties of HCP 1 and HCP 3, produced heterologously in Escherichia coli , were analyzed by electron paramagnetic resonance spectroscopy on redox‐titrated samples. Both proteins contain a [4Fe‐4S]‐cluster as well as a [4Fe‐2O‐2S]‐hybrid cluster with paramagnetic properties related to those of HCP s from Desulfovibrio species. Immunoblotting experiments combined with mass spectrometry‐based proteomics showed that both nitrate and darkness contribute to the strong upregulation of the HCP levels in C. reinhardtii growing under oxic conditions. The link to the nitrate metabolism is discussed in the light of recent data on the potential role of HCP in S‐nitrosylation in bacteria.

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