scholarly journals Study of model systems to test the potential function of Artemia group 1 late embryogenesis abundant (LEA) proteins

2015 ◽  
Vol 21 (1) ◽  
pp. 139-154 ◽  
Author(s):  
Alden H. Warner ◽  
Zhi-hao Guo ◽  
Sandra Moshi ◽  
John W. Hudson ◽  
Anna Kozarova
Keyword(s):  
Potential Function ◽  
Late Embryogenesis Abundant ◽  
Model Systems ◽  
Lea Proteins ◽  
Late Embryogenesis ◽  
Group 1

Characterization of a group 1 late embryogenesis abundant protein in encysted embryos of the brine shrimp Artemia franciscana

2009 ◽  
Vol 87 (2) ◽  
pp. 415-430 ◽  
Author(s):  
Michelle A. Sharon ◽  
Anna Kozarova ◽  
James S. Clegg ◽  
Panayiotis O. Vacratsis ◽  
Alden H. Warner
Keyword(s):  
Amino Acids ◽  
Brine Shrimp ◽  
Animal Species ◽  
Late Embryogenesis Abundant ◽  
Lea Proteins ◽  
Lea Protein ◽  
Late Embryogenesis ◽  
Its Gene ◽  
Group 1

Late embryogenesis abundant (LEA) proteins are hydrophilic molecules that are believed to function in desiccation and low-temperature tolerance in some plants and plant propagules, certain prokaryotes, and several animal species. The brine shrimp Artemia franciscana can produce encysted embryos (cysts) that enter diapause and are resistant to severe desiccation. This ability is based on biochemical adaptations, one of which appears to be the accumulation of the LEA protein that is the focus of this study. The studies described herein characterize a 21 kDa protein in encysted Artemia embryos as a group 1 LEA protein. The amino acid sequence of this protein and its gene have been determined and entered into the NCBI database (no. EF656614). The LEA protein consists of 182 amino acids and it is extremely hydrophilic, with glycine (23%), glutamine (17%), and glutamic acid (12.6%) being the most abundant amino acids. This protein also consists of 8 tandem repeats of a 20 amino acid sequence, which is characteristic of group 1 LEA proteins from non-animal species. The LEA protein and its gene are expressed only in encysted embryos and not in larvae or adults. Evidence is presented to show that the LEA protein functions in the prevention of drying-induced protein aggregation, which supports its functional role in desiccation tolerance. This report describes, for the first time, the purification and characterization of a group 1 LEA protein from an animal species.

Evolution of the Group 1 late embryogenesis abundant (Lea) genes: analysis of the Lea B19 gene family in barley

1995 ◽  
Vol 28 (6) ◽  
pp. 1039-1054 ◽  
Author(s):  
Robin A. P. Stacy ◽  
Mari Espelund ◽  
Stein S�b�e-Larssen ◽  
Kristin Hollung ◽  
Even Helliesen ◽  
...  
Keyword(s):  
Gene Family ◽  
Late Embryogenesis Abundant ◽  
Lea Genes ◽  
Late Embryogenesis ◽  
Group 1

Evidence for multiple group 1 late embryogenesis abundant proteins in encysted embryos of Artemia and their organelles

2010 ◽  
Vol 148 (5) ◽  
pp. 581-592 ◽  
Author(s):  
Alden H. Warner ◽  
Olga Miroshnychenko ◽  
Anna Kozarova ◽  
Panayiotis O. Vacratsis ◽  
Thomas H. MacRae ◽  
...  
Keyword(s):  
Late Embryogenesis Abundant ◽  
Late Embryogenesis Abundant Proteins ◽  
Multiple Group ◽  
Late Embryogenesis ◽  
Group 1

‘Dehydrin-like’ proteins and desiccation tolerance in seeds

1994 ◽  
Vol 4 (2) ◽  
pp. 135-141 ◽  
Author(s):  
O. H. Gee ◽  
R. J. Probert ◽  
S. A. Coomber
Keyword(s):  
Desiccation Tolerance ◽  
Consensus Sequence ◽  
Causal Link ◽  
Late Embryogenesis Abundant ◽  
Acer Pseudoplatanus ◽  
Lea Proteins ◽  
Late Embryogenesis ◽  
Group 2 ◽  
Plant Families ◽  
The Relationship

AbstractThe relationship between tolerance of seeds to extreme desiccation and the presence of ‘dehydrinlike’ proteins was investigated in groups of related taxa from the unrelated plant families Aceraceae and Gramineae. Dehydrin-like proteins were identified by Western blot analysis using an antibody raised against a synthetic oligopeptide representing the 23-amino acid consensus sequence common to all group 2 late-embryogenesis-abundant (LEA) proteins.Evidence is presented that seeds of Acer pseudoplatanus and A. saccharinum are desiccation intolerant (recalcitrant) whereas seeds of A. platanoides and A. rubrum are desiccation tolerant (orthodox). Despite these differences, dehydrinlike proteins at 60 and 20 kDa were detected in all four species.Dehydrins at 20 kDa were also detected in seed samples of two aquatic grasses, Porteresia coarctata and Oryza sativa from the tribe Oryzeae, despite seeds of the former rapidly losing viability on drying, whereas O. sativa is one of the best-known examples of desiccation-tolerant seeds. In O. sativa, there was a correlation between contents of dehydrins detected and the proportion of individuals capable of withstanding extreme drying. However, the possibility of a causal link between these parameters is equivocal. Dehydrin-like proteins were also detected in desiccation-sensitive seeds of Zizania palustris, Z. latifolia and Z. texana and desiccation-intolerant seeds of Spartina anglica, all from the Gramineae.The presence of group 2 LEAs is clearly not diagnostic of desiccation tolerance in seeds. However, a more direct correlation with the expression of other groups of LEAs cannot be discounted.

scholarly journals LEA13 and LEA30 Are Involved in Tolerance to Water Stress and Stomata Density in Arabidopsis thaliana

Plants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1694
Author(s):  
Abigael López-Cordova ◽  
Humberto Ramírez-Medina ◽  
Guillermo-Antonio Silva-Martinez ◽  
Leopoldo González-Cruz ◽  
Aurea Bernardino-Nicanor ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Abiotic Stress ◽  
Stress Responses ◽  
Stomatal Density ◽  
Regulatory Region ◽  
Late Embryogenesis Abundant ◽  
Stomatal Development ◽  
Lea Proteins ◽  
Late Embryogenesis ◽  
Large Protein Family

Late embryogenesis abundant (LEA) proteins are a large protein family that mainly function in protecting cells from abiotic stress, but these proteins are also involved in regulating plant growth and development. In this study, we performed a functional analysis of LEA13 and LEA30 from Arabidopsis thaliana. The results showed that the expression of both genes increased when plants were subjected to drought-stressed conditions. The insertional lines lea13 and lea30 were identified for each gene, and both had a T-DNA element in the regulatory region, which caused the genes to be downregulated. Moreover, lea13 and lea30 were more sensitive to drought stress due to their higher transpiration and stomatal spacing. Microarray analysis of the lea13 background showed that genes involved in hormone signaling, stomatal development, and abiotic stress responses were misregulated. Our results showed that LEA proteins are involved in drought tolerance and participate in stomatal density.

scholarly journals Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4930 ◽  
Author(s):  
Leidys French-Pacheco ◽  
Cesar L. Cuevas-Velazquez ◽  
Lina Rivillas-Acevedo ◽  
Alejandra A. Covarrubias ◽  
Carlos Amero
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Intrinsically Disordered Protein ◽  
Late Embryogenesis Abundant ◽  
Terminal Region ◽  
Late Embryogenesis Abundant Protein ◽  
Lea Proteins ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Late Embryogenesis

Late embryogenesis abundant (LEA) proteins accumulate in plants during adverse conditions and their main attributed function is to confer tolerance to stress. One of the deleterious effects of the adverse environment is the accumulation of metal ions to levels that generate reactive oxygen species, compromising the survival of cells. AtLEA4-5, a member of group 4 of LEAs in Arabidopsis, is an intrinsically disordered protein. It has been shown that their N-terminal region is able to undergo transitions to partially folded states and prevent the inactivation of enzymes. We have characterized metal ion binding to AtLEA4-5 by circular dichroism, electronic absorbance spectroscopy (UV–vis), electron paramagnetic resonance, dynamic light scattering, and isothermal titration calorimetry. The data shows that AtLEA4-5 contains a single binding site for Ni(II), while Zn(II) and Cu(II) have multiple binding sites and promote oligomerization. The Cu(II) interacts preferentially with histidine residues mostly located in the C-terminal region with moderate affinity and different coordination modes. These results and the lack of a stable secondary structure formation indicate that an ensemble of conformations remains accessible to the metal for binding, suggesting the formation of a fuzzy complex. Our results support the multifunctionality of LEA proteins and suggest that the C-terminal region of AtLEA4-5 could be responsible for antioxidant activity, scavenging metal ions under stress conditions while the N-terminal could function as a chaperone.

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