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- Title
Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium.
- Authors
Yadav, Shivam; Centola, Martin; Glaesmann, Mathilda; Pogoryelov, Denys; Ladig, Roman; Heilemann, Mike; Rai, L. C.; Yildiz, Özkan; Schleiff, Enrico
- 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. Cyclophilins are proteins found in many organisms, where they can play roles as chaperones, in signal transduction, or other functions. Here, Yadav et al. show that a cyanobacterial cyclophilin is involved in stress responses and in assembly of photosynthetic complexes, and displays unique structural features.
- Subjects
CYCLOPHILINS; PHYCOBILISOMES; CELLULAR signal transduction; PHOTOSYSTEMS; ARABIDOPSIS thaliana; ISOMERASES
- Publication
Nature Communications, 2022, Vol 13, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-022-29211-w