Abstract
Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a conserved protein family, displaying in vitro protective capabilities. Under water deficiency or macromolecular crowding, the N-terminal of these proteins adopts an alpha-helix conformation. This region has been identified as responsible for the protein in vitro protective activity. This study investigates whether the attainment of alpha-helix conformation and/or particular amino acid residues are required for the in vitro protective activity. The LEA4-5 protein from Arabidopsis thaliana was used to generate mutant proteins. The mutations altered conserved residues, deleted specific conserved regions, or introduced prolines to hinder alpha-helix formation. The results indicate that conserved residues are not essential for LEA4-5 protective function. Interestingly, the C-terminal region was found to contribute to this function. Moreover, alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted. Overall, LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions. These findings shed light on the in vitro mechanisms by which LEA proteins protect against water deficit stress.
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Claims 4
Claim · model-written summary
Conserved residues are not essential for LEA4-5 protective function.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae1 - Gene
- LEA4-5e0
- Outcome
- LEA4-5 protective functione0
- Qualifier
- conserved residues are not essentiale0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The results indicate that conserved residues are not essential for LEA4-5 protective function”
e1“The LEA4-5 protein from Arabidopsis thaliana”
Claim · model-written summary
The C-terminal region contributes to LEA4-5 protective function.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae1
- Gene
- LEA4-5e1
- Outcome
- LEA4-5 protective functione2
- Qualifier
- C-terminal regione0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the C-terminal region was found to contribute to this function”
e1“The LEA4-5 protein from Arabidopsis thaliana”
e2“LEA4-5 protective function”
Claim · model-written summary
Alpha-helix conformation is required for protective activity only after deletion of the C-terminal region.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae1
- Gene
- LEA4-5e1
- Outcome
- protective activitye0
- Qualifier
- only when the C-terminal region is deletede0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted”
e1“The LEA4-5 protein from Arabidopsis thaliana”
Claim · model-written summary
LEA4-5 can adopt alternative functional conformations under the tested conditions.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae1
- Gene
- LEA4-5e0
- Outcome
- alternative functional conformationse0
- Qualifier
- under the tested conditionse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions”
e1“The LEA4-5 protein from Arabidopsis thaliana”