Potential Functions of LEA Proteins from the Brine Shrimp Artemia Franciscana – Anhydrobiosis Meets Bioinformatics

Document Type

Article

Publication Date

2018

Keywords

water stress, desiccation, anhydrobiosis, state predictions, phase transitions, LEA protein, late embryogenesis abundant protein, IDP, intrinsically disordered protein, PONDR, predictor of native disorder, CH plot, charge/hydropathy plot, CDF, cumulative distribution function, MeDor, metaserver of disorder, HCA, hydrophobic cluster analysis

Digital Object Identifier (DOI)

https://doi.org/10.1080/07391102.2017.1387177

Abstract

Late embryogenesis abundant (LEA) proteins are a large group of anhydrobiosis-associated intrinsically disordered proteins, which are commonly found in plants and some animals. The brine shrimp Artemia franciscana is the only known animal that expresses LEA proteins from three, and not only one, different groups in its anhydrobiotic life stage. The reason for the higher complexity in the A. franciscana LEA proteome (LEAome), compared with other anhydrobiotic animals, remains mostly unknown. To address this issue, we have employed a suite of bioinformatics tools to evaluate the disorder status of the Artemia LEAome and to analyze the roles of intrinsic disorder in functioning of brine shrimp LEA proteins. We show here that A. franciscana LEA proteins from different groups are more similar to each other than one originally expected, while functional differences among members of group three are possibly larger than commonly anticipated. Our data show that although these proteins are characterized by a large variety of forms and possible functions, as a general strategy, A. franciscana utilizes glassy matrix forming LEAs concurrently with proteins that more readily interact with binding partners. It is likely that the function(s) of both types, the matrix-forming and partner-binding LEA proteins, are regulated by changing water availability during desiccation.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Journal of Biomolecular Structure and Dynamics, v. 36, issue 12, p. 3291-3309

Share

COinS