Some giant viruses like Mimivirus have an abundance of a small protein very rich in glycine and cysteine and which incorporates iron-sulfur (Fe-S) aggregates in the form of [2Fe-2S] type architectures, but also [3Fe-4S ] linear, a very rare arrangement in life. This protein, whose function is currently unknown, is present in all clades of Megavirinae, a subfamily of Mimiviridae, and its ability to bind Fe-S centers in an original way is a conserved property. These exploratory works published in the journal J. Am. Chem. Soc. will make it possible to address the question of the role of proteins with Fe-S centers in virology, a field very little studied to date.
This work was carried out as part of a collaboration with the Marseille (RPE) and Bordeaux (RMN) sites of Infranalytics.
reference: Evidence for [2Fe-2S]2+ and linear [3Fe-4S]1+ clusters in a unique family of glycine/cysteine-rich Fe-S proteins from Megavirinae giant viruses. Villalta, A. Srour, B. Lartigue, A. Clémancey, M. Byrne, D. Chaspoul, F. Loquet, A. Guigliarelli, B. Blondin, G. Abergel, C. Burlat, B. J Am Chem Soc 2023,145(5):2733-2738. doi: 10.1021/jacs.2c10484.
Contact :
Bénédicte Burlat, Lecturer Aix-Marseille University
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Bioenergetics and protein engineering laboratory (CNRS / AMU)
BIP - UMR 7281, Mediterranean Microbiology Institute - IMM - FR 3479, IM2B
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Chantal Abergel, DR CNRS
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Genomic and Structural Information Laboratory, (CNRS / AMU)
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