LEA Proteins and the Evolution of the WHy Domain

The late embryogenesis abundant (LEA) family is composed of a diverse collection of multidomain and multifunctional proteins found in all three domains of the tree of life, but they are particularly common in plants. Most members of the family are known to play an important role in abiotic stress re...

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Bibliographic Details
Published in:Applied and environmental microbiology 2018-08, Vol.84 (15)
Main Authors: Mertens, Jasmin, Aliyu, Habibu, Cowan, Don A
Format: Article
Language:English
Subjects:
Amino acid sequence
Archaea
Bacteria
Biopolymer denaturation
E coli
Embryogenesis
Embryonic growth stage
Eukaryotes
Gene transfer
Genomes
Genotype & phenotype
Harbors
Hypersensitive response
LEA protein
Minireview
Phenotypes
Phylogenetics
Phylogeny
Protein denaturation
Proteins
Structure-function relationships
Water stress
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Summary:The late embryogenesis abundant (LEA) family is composed of a diverse collection of multidomain and multifunctional proteins found in all three domains of the tree of life, but they are particularly common in plants. Most members of the family are known to play an important role in abiotic stress response and stress tolerance in plants but are also part of the plant hypersensitive response to pathogen infection. The mechanistic basis for LEA protein functionality is still poorly understood. The group of LEA 2 proteins harbor one or more copies of a unique domain, the ater stress and persensitive response (WHy) domain. This domain sequence has recently been identified as a unique open reading frame (ORF) in some bacterial genomes (mostly in the phylum ), and the recombinant bacterial WHy protein has been shown to exhibit a stress tolerance phenotype in and an protein denaturation protective function. Multidomain phylogenetic analyses suggest that the WHy protein gene sequence may have ancestral origins in the domain , with subsequent acquisition in and eukaryotes via endosymbiont or horizontal gene transfer mechanisms. Here, we review the structure, function, and nomenclature of LEA proteins, with a focus on the WHy domain as an integral component of the LEA constructs and as an independent protein.
ISSN:0099-2240
1098-5336
DOI:10.1128/AEM.00539-18