Role of Plasticity and Disorder in Protein Moonlighting: Blurring of Lines Between Biocatalysts and Other Biologically Active Proteins

Document Type

Book Chapter

Publication Date

2023

Keywords

Moonlighting Proteins, Multifunctional Proteins, Multitasking Proteins, Conformational Diversity, Structural Heterogeneity, Intrinsically Disordered Protein, Binding Promiscuity, Structure–function Continuum

Digital Object Identifier (DOI)

https://doi.org/10.1016/B978-0-323-99533-7.00003-0

Abstract

In the new view of proteins, “one sequence–one structure–one function” paradigm has been replaced by “one sequence–conformational ensemble–many functions.” Driving this new paradigm is multispecificity of proteins coupled with their plasticity and intrinsic disorder. Moonlighting, an important basis of protein multispecificity, blurs the distinction between enzymes and noncatalytic proteins. Many enzymes can moonlight as regulatory proteins. Moonlighting activity can depend upon the cell type, cellular localization, oligomerization status, and concentration of the ligands around the protein. Moonlighting helps in keeping the genome small and is found in proteins from archaea, prokaryotes, and eukaryotes. This chapter discusses the roles of moonlighting in both health and diseases. Examples of the former include chaperones, unconventional secretion pathways, 14-3-3 proteins, and ribosomal proteins. The virulence activity of pathogens also involves moonlighting in several cases. Irrespective of the physiological role played by moonlighting, both plasticity and disorder are involved.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Role of Plasticity and Disorder in Protein Moonlighting: Blurring of Lines Between Biocatalysts and Other Biologically Active Proteins, in M. N. Gupta & V. N. Uversky (Eds.), Structure and Intrinsic Disorder in Enzymology, Academic Press, p. 279-301

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