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05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
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Functional amyloid: widespread in Nature, diverse in purpose
Chi L L Pham1, Ann H Kwan2, Margaret Sunde
1*Discipline of Pharmacology, School of Medical Sciences, University of Sydney, NSW 2006, Australia.
Essays in Biochemistry
|August 19, 2014
Summary
Functional amyloids, initially linked to disease, are now recognized for diverse biological roles across organisms. This chapter explores their functions, assembly, and the strategies organisms use to manage their potential toxicity.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Amyloids are insoluble protein deposits with a cross-β structure.
- Initially associated with human diseases, amyloids are now known to have diverse biological functions.
- These functions span from structural support to epigenetic inheritance.
Purpose of the Study:
- To discuss functional amyloids across various organisms (microbes, animals, mammals).
- To detail their biological roles, molecular composition, and assembly processes.
- To explore organismal strategies for managing functional amyloid toxicity.
Main Methods:
- Literature review and synthesis of existing research on functional amyloids.
- Analysis of diverse examples from microorganisms to mammals.
- Discussion of molecular mechanisms and biological implications.
Main Results:
- Functional amyloids serve roles in structure, protection, cell recognition, protein control, and inheritance.
- Examples include curli, silks, chaplins, Sup35, and CPEB (cytoplasmic polyadenylation element-binding protein).
- Amyloids are also implicated in signal transduction and host defense.
Conclusions:
- The cross-β structure of amyloids is a versatile motif utilized for numerous biological functions.
- Understanding functional amyloids expands our view beyond disease pathology.
- Organisms have evolved mechanisms to harness and control these protein structures.
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