Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium

Shivam Yadav, Martin Centola, Mathilda Glaesmann, Denys Pogoryelov, Roman Ladig, Mike Heilemann, L. C. Rai, Özkan Yildiz and Enrico Schleiff ()
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Shivam Yadav: Goethe University Frankfurt
Martin Centola: Max-Planck-Institute of Biophysics
Mathilda Glaesmann: Goethe University
Denys Pogoryelov: Goethe University Frankfurt
Roman Ladig: Goethe University Frankfurt
Mike Heilemann: Goethe University
L. C. Rai: Banaras Hindu University
Özkan Yildiz: Max-Planck-Institute of Biophysics
Enrico Schleiff: Goethe University Frankfurt

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Cyclophilins, or immunophilins, are proteins found in many organisms including bacteria, plants and humans. Most of them display peptidyl-prolyl cis-trans isomerase activity, and play roles as chaperones or in signal transduction. Here, we show that cyclophilin anaCyp40 from the cyanobacterium Anabaena sp. PCC 7120 is enzymatically active, and seems to be involved in general stress responses and in assembly of photosynthetic complexes. The protein is associated with the thylakoid membrane and interacts with phycobilisome and photosystem components. Knockdown of anacyp40 leads to growth defects under high-salt and high-light conditions, and reduced energy transfer from phycobilisomes to photosystems. Elucidation of the anaCyp40 crystal structure at 1.2-Å resolution reveals an N-terminal helical domain with similarity to PsbQ components of plant photosystem II, and a C-terminal cyclophilin domain with a substrate-binding site. The anaCyp40 structure is distinct from that of other multi-domain cyclophilins (such as Arabidopsis thaliana Cyp38), and presents features that are absent in single-domain cyclophilins.

Date: 2022
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DOI: 10.1038/s41467-022-29211-w

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