Phylogenomic and structural modeling analyses of the PsbP superfamily reveal multiple small segment additions in the evolution of photosystem II-associated PsbP protein in green plants

書誌事項

公開日
2010-07
権利情報
  • https://www.elsevier.com/tdm/userlicense/1.0/
DOI
  • 10.1016/j.ympev.2009.11.021
公開者
Elsevier BV

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説明

PsbP is a thylakoid lumen protein involved in oxygen evolution in photosystem II (PSII) in green plants. Genomic analysis identified a number of PsbP homologs in plants, algae, and cyanobacteria. To analyze the transition of cyanobacterial PsbO/U/V complex to PsbO/P/Q complex in green plants, the evolutionary history of the PsbP superfamily was reconstructed. Phylogenetic analyses suggested that PsbP homologs be classified into eight major families (A-H), which were also characterized by specific insertion/deletion of short segments, as found by sequence alignment and homology modeling. Family A represented authentic PsbP proteins involved in oxygen evolution. The cyanobacterial PsbP and plant/algal PPL (Family H), having the simplest structure, should be considered as the root of all other families of PsbP, which subsequently gained various short, family-specific structural motifs during diversification of PsbP families. Interestingly, segments specific to Family A proteins were found arranged as a ring surrounding the modeled Arabidopsis PsbP protein. These results suggest that Family A-specific additions of short segments played a decisive role in the transition of PsbO/U/V to PsbO/P/Q complex in green plants.

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