Special Issue "Protein-Based Infection, Inheritance, and Memory"
Deadline for manuscript submissions: 31 January 2022.
2. Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg 199034, Russia
Interests: yeast genetics; protein biosynthesis, misfolding and aggregation; protein quality control; amyloids; prions; chaperones and stress response; protein-based inheritance
Interests: prion; amyloid; protein structure; proteomics; yeast; bacteria; protein aggregate; chaperone; protein fibril; amyloidogenic region
Overwhelming evidence, mostly accumulated relatively recently, has demonstrated that the templated proliferation of protein isoforms can result in the reproduction and amplification of information encoded in the protein structure. Therefore, self-perpetuating protein isoforms can become carriers of biological information that are not directly encoded in DNA sequences. Transmissible protein isoforms (prions) manifest themselves as infectious agents causing diseases, including some devastating diseases in humans and other mammals. In yeast and other fungi, prions manifest themselves as heritable elements, transmitted via cytoplasm. At the molecular level, many prions are based on fibrous cross-β aggregates (amyloids), although other molecular mechanisms for the transmission of protein-based information are also being uncovered. Self-perpetuating protein isoforms have also been implicated in cellular memory. Such non-heritable molecular memory devices found in yeast have been termed mnemons. The ability of proteins to serve as information templates challenges existing biological paradigms and opens additional pathways for information transfer in biological systems, potentially playing a role in adaptation and evolution. The current issue will cover molecular mechanisms controlling the ability of proteins to serve as information carriers in infection, inheritance, and memory.
Prof. Dr. Yury O. Chernoff
Dr. Anton Nizhnikov
Manuscript Submission Information
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- non-Mendelian inheritance
- protein conformation