Cryoprotective activity of Arabidopsis KS-type dehydrin depends on the hydrophobic amino acids of two active segments

Yokoyama, Tomoka; Ohkubo, Tomohiro; Kamiya, Keita; Hara, Masakazu

doi:10.1016/j.abb.2020.108510

Cited by 23 publications

(26 citation statements)

References 60 publications

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“…This was absent in the shuffled D-segment, indicating the significant role played by the specific organization of D-segment amino acid residues in inducing the helical backbone. As previously reported, the K-segments in AtHIRD11 and AtLEA4 dehydrins were responsible for promoting helix transition ( 18 , 42 ). Our study reports a similar α-helix gaining tendency of the D-segments in the presence of TFE.…”

Section: Discussionsupporting

confidence: 74%

“…The D-segment, with the sequence motif EGφφD(R/K)AKDAφ, where φ is a hydrophobic residue, showed amphipathic α-helix gaining propensity, similar to the K-segment. Decades of research on DHNs have shown the K-segment to be one important factor behind DHN function ( 13 , 15 , 41 , 42 ). The K-segment has been shown to adopt an amphipathic α-helix organization under water-deficit stress conditions ( 1 ).…”

Section: Discussionmentioning

confidence: 99%

“…A similar conclusion was drawn from a study with wheat DHN-5 deletion mutant ( 41 ). Recent studies with Arabidopsis DHN have pointed toward the amphipathic α-helical organization of the K-segment as an important aspect for LDH protection ( 13 , 42 ). Not just the K-segment, DHN size has also been found to be correlated with the degree of functional protection provided to LDH under stress ( 23 , 39 ).…”

Section: Discussionmentioning

confidence: 99%

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Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation

Upadhyaya

Das

Basu

et al. 2021

Journal of Biological Chemistry

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Plants use a diverse set of proteins to mitigate various abiotic stresses. The intrinsically disordered protein dehydrin is an important member of this repertoire of proteins, characterized by a canonical amphipathic K-segment. It can also contain other stress-mitigating noncanonical segments—a likely reflection of the extremely diverse nature of abiotic stress encountered by plants. Among plants, the poikilohydric mosses have no inbuilt mechanism to prevent desiccation and therefore are likely to contain unique noncanonical stress-responsive motifs in their dehydrins. Here we report the recurring occurrence of a novel amphipathic helix-forming segment (D-segment: EGφφD(R/K)AKDAφ, where φ represents a hydrophobic residue) in Physcomitrella patens dehydrin (PpDHNA), a poikilohydric moss. NMR and CD spectroscopic experiments demonstrated the helix-forming tendency of the D-segment, with the shuffled D-segment as control. PpDHNA activity was shown to be size as well as D-segment dependent from in vitro , in vivo , and in planta studies using PpDHNA and various deletion mutants. Bimolecular fluorescence complementation studies showed that D-segment-mediated PpDHNA self-association is a requirement for stress abatement. The D-segment was also found to occur in two rehydrin proteins from Syntrichia ruralis , another poikilohydric plant like P. patens . Multiple occurrences of the D-segment in poikilohydric plant dehydrins/rehydrins, along with the experimental demonstration of the role of D-segment in stress abatement, implies that the D-segment mediates unique resurrection strategies, which may be employed by plant dehydrins that are capable of mitigating extreme stress.

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Section: Discussionsupporting

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation

Upadhyaya

Das

Basu

et al. 2021

Journal of Biological Chemistry

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“…Importantly, Yokoyama et al (2020) have recently showed that both the K-and the H-segments (which the authors called K and NK1, respectively) of AtHIRD11 can protect proteins from freezing damage with similar efficiencies. Structurally, the presence of the K-and H-segments were needed for AtHIRD11 to transition from a disordered to an ordered state 65 . Overall, the functional results by Yokoyama et al (2020) show that the H-segment is an important component of H-DHNs, as implied by its high degree of phylogenetic conservation, and suggests that K-and H-segments might play overlapping roles in the activity of H-DHNs.…”

Section: Discussionmentioning

confidence: 99%

“…Structurally, the presence of the K-and H-segments were needed for AtHIRD11 to transition from a disordered to an ordered state 65 . Overall, the functional results by Yokoyama et al (2020) show that the H-segment is an important component of H-DHNs, as implied by its high degree of phylogenetic conservation, and suggests that K-and H-segments might play overlapping roles in the activity of H-DHNs.…”

Section: Discussionmentioning

confidence: 99%

Genomic diversification of dehydrin gene family in vascular plants: three distinctive orthologue groups and a novel KS-dehydrin conserved protein motif

2021

Preprint

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Dehydrins (DHNs) are a family of plant proteins that play important roles on abiotic stress tolerance and seed development. They are classified into five structural subgroups: K-, SK-, YK-, YSK-, and KS-DHNs, according to the presence of conserved motifs named K-, Y- and S- segments.We carried out a comparative structural and phylogenetic analysis of these proteins, focusing on the less-studied KS-type DHNs. A search for conserved motifs in DHNs from 56 plant genomes revealed that KS-DHNs possess a unique and highly conserved N-terminal, 15-residue amino acid motif not previously described. This novel motif, that we named H-segment, is present in DHNs of angiosperms, gymnosperms and lycophytes, suggesting that HKS-DHNs were present in the first vascular plants. Phylogenetic and microsynteny analyses indicate that the five structural subgroups of angiosperm DHNs can be assigned to three groups of orthologue genes, characterized by the presence of the H-, F- or Y- segments. Importantly, the hydrophilin character of DHNs correlate with the phylogenetic origin of the DHNs rather than to the traditional structural subgroups. We propose that angiosperm DHNs can be ultimately subdivided into three orthologous groups, a phylogenetic framework that should help future studies on the evolution and function of this protein family.

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Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

Hernández‐Sánchez,

Rindfleisch,

Alpers

et al. 2024

Protein Science

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Intrinsically disordered late embryogenesis abundant (LEA) proteins play a central role in the tolerance of plants and other organisms to dehydration brought upon, for example, by freezing temperatures, high salt concentration, drought or desiccation, and many LEA proteins have been found to stabilize dehydration‐sensitive cellular structures. Their conformational ensembles are highly sensitive to the environment, allowing them to undergo conformational changes and adopt ordered secondary and quaternary structures and to participate in formation of membraneless organelles. In an interdisciplinary approach, we discovered how the functional diversity of the Arabidopsis thaliana LEA protein COR15A found in vitro is encoded in its structural repertoire, with the stabilization of membranes being achieved at the level of secondary structure and the stabilization of enzymes accomplished by the formation of oligomeric complexes. We provide molecular details on intra‐ and inter‐monomeric helix–helix interactions, demonstrate how oligomerization is driven by an α‐helical molecular recognition feature (α‐MoRF) and provide a rationale that the formation of noncanonical, loosely packed, right‐handed coiled‐coils might be a recurring theme for homo‐ and hetero‐oligomerization of LEA proteins.

show abstract

Cryoprotective activity of Arabidopsis KS-type dehydrin depends on the hydrophobic amino acids of two active segments

Cited by 23 publications

References 60 publications

Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation

Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation

Genomic diversification of dehydrin gene family in vascular plants: three distinctive orthologue groups and a novel KS-dehydrin conserved protein motif

Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

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