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Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures Wickner RB; Shewmaker F; Kryndushkin D; Edskes HKBioessays 2008[Oct]; 30 (10): 955-64Most prions (infectious proteins) are self-propagating amyloids (filamentous protein multimers), and have been found in both mammals and fungal species. The prions [URE3] and [PSI+] of yeast are disease agents of Saccharomyces cerevisiae while [Het-s] of Podospora anserina may serve a normal cellular function. The parallel in-register beta-sheet structure shown by prion amyloids makes possible a templating action at the end of filaments which explains the faithful transmission of variant differences in these molecules. This property of self-reproduction, in turn, allows these proteins to act as de facto genes, encoding heritable information.|Amyloid/*chemistry/genetics/ultrastructure[MESH]|Glutathione Peroxidase[MESH]|Peptide Termination Factors[MESH]|Podospora/*chemistry/genetics[MESH]|Prions/*chemistry/genetics/ultrastructure[MESH]|Protein Structure, Secondary[MESH]|Saccharomyces cerevisiae Proteins/*chemistry/genetics/ultrastructure[MESH]|Saccharomyces cerevisiae/*chemistry/genetics[MESH] |
