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キーワード:
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要旨:
Programmed cell death (PCD) is a mechanism linked to multicellularity. Existing research suggests that ex- tensively studied PCD proteins found in eukaryotes share homology with certain prokaryotic proteins that hitherto have not been fully characterized. Putative PCD apparatus consists of two co-expressed proteins - Wrap1 and Npun_R6613, which complex structure nor coevolution has yet been determined. Therefore, using bioinformatics approach - AlphaFold2 folding, protein-protein molecular docking, protein in- terface and sequence analysis we managed to determine structure of Wrap1-Npun_R6613 complex and annotated coevolution of selected residues of both proteins. Our study indicate that it exists as tetradecameric structure, with Wrap1 bound to the membrane, while Npun_R6613 counterpart is non-covalently bound through several interface residues. It extends present knowledge of mechanisms and evolution of programmed cell death in bacteria. The next step is the experimental part, which are going to be conducted on yeast.
