A Group 6 Late Embryogenesis Abundant Protein from Common Bean Is a Disordered Protein with Extended Helical Structure and Oligomer-forming Properties

Rivera-Najera, Lucero Y.; Saab‐Rincón, Gloria; Battaglia, Marina; Amero, Carlos; Pulido, Nancy O.; García‐Hernández, Enrique; Solórzano, Rosa M.; Reyes, José Luis; Covarrubias, Alejandra A.

doi:10.1074/jbc.m114.583369

Cited by 43 publications

(45 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We did not find evidence of extended helical conformations (e.g. poly-L-proline II) for any of these proteins, such as those found in LEA groups 1, 2, and 6 (10,39). Altogether, these data demonstrate that AtLEA4 proteins are IDPs with residual ␣-helix structure in aqueous solution.…”

Section: A Thaliana Group 4 Late Embryogenesis Abundant Proteins Arementioning

confidence: 50%

“…The composition of these proteins is also characteristic of a group of proteins known as intrinsically disordered proteins (IDPs) (5,6). Consistent with the predicted structural disorder for most LEA proteins, structural analyses have confirmed this property for some of them in aqueous solution (7)(8)(9)(10)(11)(12)(13). Based on their sequence similarity, LEA proteins have been classified in seven groups or families, each one characterized by the presence of specific sequence motifs (2).…”

mentioning

confidence: 76%

See 1 more Smart Citation

The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit

Cuevas-Velazquez

Saab‐Rincón

Reyes

et al. 2016

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Late embryogenesis abundant (LEA) proteins are a conserved group of proteins widely distributed in the plant kingdom that participate in the tolerance to water deficit of different plant species. In silico analyses indicate that most LEA proteins are structurally disordered. The structural plasticity of these proteins opens the question of whether water deficit modulates their conformation and whether these possible changes are related to their function. In this work, we characterized the secondary structure of Arabidopsis group 4 LEA proteins. We found that they are disordered in aqueous solution, with high intrinsic potential to fold into ␣-helix. We demonstrate that complete dehydration is not required for these proteins to sample ordered structures because milder water deficit and macromolecular crowding induce high ␣-helix levels in vitro, suggesting that prevalent conditions under water deficit modulate their conformation. We also show that the N-terminal region, conserved across all group 4 LEA proteins, is necessary and sufficient for conformational transitions and that their protective function is confined to this region, suggesting that folding into ␣-helix is required for chaperone-like activity under water limitation. We propose that these proteins can exist as different conformers, favoring functional diversity, a moonlighting property arising from their structural dynamics.

show abstract

Section: A Thaliana Group 4 Late Embryogenesis Abundant Proteins Arementioning

confidence: 50%

mentioning

confidence: 76%

The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit

Cuevas-Velazquez

Saab‐Rincón

Reyes

et al. 2016

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Motifs 1 to 5 were detected in AcLEA wherein the motif arrangement is M4-M5-M3-M1-M2 with only one complete motif of each type ( Figure 1A ). On the other hand, the motifs arrangement for LEA group 6 is in the order M3-M1-M2-M4 (Rivera-Najera et al, 2014). …”

Section: Resultsmentioning

confidence: 99%

“…It is well established that TFE can induce α-helix folding in peptides (Buck, 1998; Boswell et al, 2014), as well as in unstructured proteins with a predisposition to form secondary structure such as LEA proteins (Shih et al, 2004; Rivera-Najera et al, 2014). Therefore the effect of TFE was evaluated on the rAcLEA conformation.…”

Section: Resultsmentioning

confidence: 99%

Insights on Structure and Function of a Late Embryogenesis Abundant Protein from Amaranthus cruentus: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress

et al. 2017

View full text Add to dashboard Cite

Late embryogenesis abundant (LEA) proteins are part of a large protein family that protect other proteins from aggregation due to desiccation or osmotic stresses. Recently, the Amaranthus cruentus seed proteome was characterized by 2D-PAGE and one highly accumulated protein spot was identified as a LEA protein and was named AcLEA. In this work, AcLEA cDNA was cloned into an expression vector and the recombinant protein was purified and characterized. AcLEA encodes a 172 amino acid polypeptide with a predicted molecular mass of 18.34 kDa and estimated pI of 8.58. Phylogenetic analysis revealed that AcLEA is evolutionarily close to the LEA3 group. Structural characteristics were revealed by nuclear magnetic resonance and circular dichroism methods. We have shown that recombinant AcLEA is an intrinsically disordered protein in solution even at high salinity and osmotic pressures, but it has a strong tendency to take a secondary structure, mainly folded as α-helix, when an inductive additive is present. Recombinant AcLEA function was evaluated using Escherichia coli as in vivo model showing the important protection role against desiccation, oxidant conditions, and osmotic stress. AcLEA recombinant protein was localized in cytoplasm of Nicotiana benthamiana protoplasts and orthologs were detected in seeds of wild and domesticated amaranth species. Interestingly AcLEA was detected in leaves, stems, and roots but only in plants subjected to salt stress. This fact could indicate the important role of AcLEA protection during plant stress in all amaranth species studied.

show abstract

“…2 Suppl.), eliminating the effect of photoperiod or circadian rhythm on their expression patterns. Most LEA proteins remained soluble after being heated because they are intrinsically unstructured (Receveur-Bréchot et al 2006, Rivera-Najera et al 2014. To assess the stability of heat-treated LEA proteins, the three MtLEA proteins encoded by the tandemly aligned loci on chromosome 7 from genotype R108 and a full-length mutant version of LEA3140, LEA3140M (Fig.…”

Section: Resultsmentioning

confidence: 99%

Three tandemly aligned LEA genes from Medicago truncatula confer differential protection to Escherichia coli against abiotic stresses

Zhang¹,

Wang²,

Liu³

et al. 2020

Biol. plant.

View full text Add to dashboard Cite

Late embryogenesis abundant (LEA) proteins are important for abiotic stress tolerance in diverse organisms. Within the LEA protein superfamily, group 4 members are characterized by a conserved N-terminal region and a structurally disordered C-terminal region that varies regarding length and amino acid content. Previous in vitro assays have suggested that the conserved N-terminal region shared by group 4 LEA proteins is critical for forming an amphipathic α-helix and protecting enzymatic activities from the adverse effects of desiccation or freezing. However, the cellular roles of the varying C-terminal region remain largely to be characterized. Medicago truncatula contains five subgroup LEA4B proteins encoding loci of which three are tandemly arranged on chromosome 7 due to local gene duplication events. In this study, abiotic stresses and addition of abscisic acid (ABA) induced the transcription of the four LEA4B genes. Escherichia coli cells overexpressing the three tandemly aligned LEA genes indicated significantly increased tolerance to salt, osmotic, heat, and freezing stresses. However, the extent of the protective effects on the survival and growth of bacterial cells differed among the LEA proteins, potentially because of variations in the C-terminal region. This possibility was further supported by the observation that the protective effects of the native truncated MtLEA3140, which only contains a conserved N-terminal region, were inferior to the effects of the full-length mutant version. The results suggest that the structurally flexible C-terminal region of group 4 LEA proteins plays roles in protecting cells from damages caused by various abiotic stresses, and provide clues for elucidating the mechanisms underlying the intracellular functions of these proteins.

show abstract

A Group 6 Late Embryogenesis Abundant Protein from Common Bean Is a Disordered Protein with Extended Helical Structure and Oligomer-forming Properties

Cited by 43 publications

References 73 publications

The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit

The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit

Insights on Structure and Function of a Late Embryogenesis Abundant Protein from Amaranthus cruentus: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress

Three tandemly aligned LEA genes from Medicago truncatula confer differential protection to Escherichia coli against abiotic stresses

Contact Info

Product

Resources

About