Late Embryogenesis Abundant Protein–Client Protein Interactions

Dirk, Lynnette M.A.; Abdel, Caser G.; Ahmad, Imran; Neta, Izabel Costa Silva; Pereira, Cristiane Carvalho; Pereira, Francisco Élder Carlos Bezerra; Unêda-Trevisoli, Sandra Helena; Pinheiro, Daniel Guariz; Downie, A. Bruce

doi:10.3390/plants9070814

Cited by 25 publications

(33 citation statements)

References 167 publications

(230 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dehydrins are considered as molecular protectors by interacting with protective target proteins against different abiotic stress (Dirk et al., 2020). Based on a screen to identify potential interaction proteins of MsDHN1, two AQPs (MsPIP2;1 and MsTIP1;1) were proven to interact with MsDHN1 using Y2H, BiFC and Co‐IP (Figure 4).…”

Section: Discussionmentioning

confidence: 99%

Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativaL.) by affecting oxalate exudation from root tips

Wen

Fan

et al. 2021

The Plant Journal

View full text Add to dashboard Cite

SUMMARY A SK3‐type dehydrin MsDHN1 was cloned from alfalfa (Medicago sativa L.). Its function and gene regulatory pathways were studied via overexpression and suppression of MsDHN1 in alfalfa seedlings or hairy roots. The results showed that MsDHN1 is a typical intrinsically disordered protein that exists in the form of monomers and homodimers in alfalfa. The plant growth rates increased as a result of MsDHN1 overexpression (MsDHN1‐OE) and decreased upon MsDHN1 suppression (MsDHN1‐RNAi) in seedlings or hairy roots of alfalfa compared with the wild‐type or the vector line under Al stress. MsDHN1 interacting with aquaporin (AQP) MsPIP2;1 and MsTIP1;1 positively affected oxalate secretion from root tips and Al accumulation in root tips. MsABF2 was proven to be an upstream transcription factor of MsDHN1 and activated MsDHN1 expression by binding to the ABRE element of the MsDHN1 promoter. The transcriptional regulation of MsABF2 on MsDHN1 was dependent on the abscisic acid signaling pathway. These results indicate that MsDHN1 can increase alfalfa tolerance to Al stress via increasing oxalate secretion from root tips, which may involve in the interaction of MsDHN1 with two AQP.

show abstract

Section: Discussionmentioning

confidence: 99%

Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativaL.) by affecting oxalate exudation from root tips

Wen

Fan

et al. 2021

The Plant Journal

View full text Add to dashboard Cite

show abstract

“…dehydrated cells (30). However, previous bioinformatics analysis of AfrLEA6 also identified sequence features associated with proteins known to undergo LLPS to form membraneless organelles (MLOs), which warranted a more thorough evaluation on the possible role of LLPS in animal anhydrobiosis (14,27,31,32).…”

Section: Significancementioning

confidence: 99%

Liquid-liquid phase separation promotes animal desiccation tolerance

Belott

Janis

Menze

2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Proteinaceous liquid-liquid phase separation (LLPS) occurs when a polypeptide coalesces into a dense phase to form a liquid droplet (i.e., condensate) in aqueous solution. In vivo, functional protein-based condensates are often referred to as membraneless organelles (MLOs), which have roles in cellular processes ranging from stress responses to regulation of gene expression. Late embryogenesis abundant (LEA) proteins containing seed maturation protein domains (SMP; PF04927) have been linked to storage tolerance of orthodox seeds. The mechanism by which anhydrobiotic longevity is improved is unknown. Interestingly, the brine shrimp Artemia franciscana is the only animal known to express such a protein (AfrLEA6) in its anhydrobiotic embryos. Ectopic expression of AfrLEA6 (AWM11684) in insect cells improves their desiccation tolerance and a fraction of the protein is sequestered into MLOs, while aqueous AfrLEA6 raises the viscosity of the cytoplasm. LLPS of AfrLEA6 is driven by the SMP domain, while the size of formed MLOs is regulated by a domain predicted to engage in protein binding. AfrLEA6 condensates formed in vitro selectively incorporate target proteins based on their surface charge, while cytoplasmic MLOs formed in AfrLEA6-transfected insect cells behave like stress granules. We suggest that AfrLEA6 promotes desiccation tolerance by engaging in two distinct molecular mechanisms: by raising cytoplasmic viscosity at even modest levels of water loss to promote cell integrity during drying and by forming condensates that may act as protective compartments for desiccation-sensitive proteins. Identifying and understanding the molecular mechanisms that govern anhydrobiosis will lead to significant advancements in preserving biological samples.

show abstract

“…In vitro evidence suggested that LEA proteins ensure enzyme activity, act as a molecular shield preventing protein aggregation and as chaperone, stabilize and associate with membranes, sequester ions and reactive oxygenic species, prevent cellular water loss by acting as hydration buffer, and stabilize sugar glasses by increasing the glass transition temperature [ 4 , 5 , 12 , 14 , 17 ]. In addition, the IDP-structure of LEA proteins might contribute to a phenomenon named liquid-liquid phase separation (LLPS), a process which gives rise to proteinaceous membrane-less organelles [ 18 ]. Nevertheless, not all IDPs undergo LLPS and intrinsically disordered regions (IDRs) are not necessarily required for LLPS.…”

Section: Introductionmentioning

confidence: 99%

“…LEA proteins are able to interact with each other or other proteins. Direct LEA-target protein interactions have been shown among the LEA_2, dehydrin, LEA_4, and the SMP protein families [ 18 ]. As an example, dehydrins AtCOR47, AtERD10, and AtRAB18 bound to the aquaporin AtPIP2B and a homodimeric interaction of RAB18 complexes was revealed as well as a heterodimeric association between AtRAB18 acidic dehydrins [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

“…As an example, dehydrins AtCOR47, AtERD10, and AtRAB18 bound to the aquaporin AtPIP2B and a homodimeric interaction of RAB18 complexes was revealed as well as a heterodimeric association between AtRAB18 acidic dehydrins [ 19 ]. Moreover, associates of COR15A with the small and large subunit of Rubisco, potentially prevented a freezing induced deactivation of the enzyme [ 18 ]. Two other dehydrins from Arabidopsis, ERD14 (At1g76180), and HIRD11 (At1g54410) interacted with the Arabidopsis Phi9 Glutathione-S-Transferase9 and the Arabidopsis leucine-rich repeat receptor-like kinase (LRR-RLK) Phloem Intercalated with Xylem-Like 1 (AtPXL1), respectively [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers

et al. 2021

View full text Add to dashboard Cite

LEA proteins are involved in plant stress tolerance. In Arabidopsis, the LEA_4 Pfam group is the biggest group with the majority of its members being expressed in dry seeds. To assess subcellular localization in vivo, we investigated 11 seed-expressed LEA_4 proteins in embryos dissected from dry seeds expressing LEA_4 fusion proteins under its native promoters with the Venus fluorescent protein (proLEA_4::LEA_4:Venus). LEA_4 proteins were shown to be localized in the endoplasmic reticulum, nucleus, mitochondria, and plastids. LEA9, in addition to the nucleus, was also found in cytoplasmic condensates in dry seeds dependent on cellular hydration level. Most investigated LEA_4 proteins were detected in 4-d-old seedlings. In addition, we assessed bioinformatic tools for predicting subcellular localization and promoter motifs of 11 seed-expressed LEA_4 proteins. Ratiometric bimolecular fluorescence complementation assays showed that LEA7, LEA29, and LEA48 form homodimers while heterodimers were formed between LEA7-LEA29 and LEA42-LEA48 in tobacco leaves. Interestingly, LEA48 homodimers and LEA42-LEA48 heterodimers formed droplets structures with liquid-like behavior. These structures, along with LEA9 cytoplasmic condensates, may have been formed through liquid-liquid phase separation. These findings suggest possible important roles of LLPS for LEA protein functions.

show abstract

Late Embryogenesis Abundant Protein–Client Protein Interactions

Cited by 25 publications

References 167 publications

Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativaL.) by affecting oxalate exudation from root tips

Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativaL.) by affecting oxalate exudation from root tips

Liquid-liquid phase separation promotes animal desiccation tolerance

Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers

Contact Info

Product

Resources

About