期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 430, 期 23, 页码 4607-4618出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.07.017
关键词
prions; protein aggregation; chaperones
资金
- National Institutes of Health New Innovator Award [NIH-DP2-GM119140]
- NSF-CAREER Award [MCB1453762]
- David and Lucile Packard Foundation
- Damon Runyon Cancer Research Foundation [DRG2221-15]
A central tenet of molecular biology is that heritable information is stored in nucleic acids. However, this paradigm has been overturned by a group of proteins called prions. Prion proteins, many of which are intrinsically disordered, can adopt multiple conformations, at least one of which has the capacity to self template. This unusual folding landscape drives a form of extreme epigenetic inheritance that can be stable through both mitotic and meiotic cell divisions. Although the first prion discovered-mammalian PrP-is the causative agent of debilitating neuropathies, many additional prions have now been identified that are not obviously detrimental and can even be adaptive. Intrinsically disordered regions, which endow proteins with the bulk property of phase-separation, can also be drivers of prion formation. Indeed, many protein domains that promote phase separation have been described as prion-like. In this review, we describe how prions lie at the crossroads of phase separation, epigenetic inheritance, and evolutionary adaptation. (C) 2018 Elsevier Ltd. All rights reserved.
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