Solution structure of a late embryogenesis abundant protein (LEA14) from <i>Arabidopsis thaliana</i>, a cellular stress‐related protein

Singh, Shanteri; Cornilescu, Claudia C.; Tyler, Robert C.; Cornilescu, Gabriel; Tonelli, Marco; Lee, Min S.; Markley, John L.

doi:10.1110/ps.051579205

Cited by 111 publications

(81 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The data on the secondary structure of MtEm6 and MtPM25 in solution complement those obtained for members of groups 3 and 4 using FTIR spectroscopy as well as for dehydrins and a member of the D95 family with other spectroscopy techniques. In the hydrated state, LEA proteins exhibit a wide degree of disorder, ranging from unordered (group 1; Soulages et al, 2002; group 3 LEA proteins from Typha latifolia pollen [Wolkers et al, 2001]; nematodes [Goyal et al, 2003]; and dehydrins [Soulages et al, 2003]), to 60% to 70% unordered (GmPM16, a soybean group 4 LEA protein [Shih et al, 2004] and Em proteins [Table IV;McCubbin et al, 1985]), and finally down to 50% unordered (MtPM25 [Table IV] and an Arabidopsis Lea14, a member of the D 95 family [PF03168; Singh et al, 2005]). Likewise, the nature and contents of ordered structures in solution varies greatly.…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

et al. 2006

View full text Add to dashboard Cite

A proteomic analysis was performed on the heat stable protein fraction of imbibed radicles of Medicago truncatula seeds to investigate whether proteins can be identified that are specifically linked to desiccation tolerance (DT). Radicles were compared before and after emergence (2.8 mm long) in association with the loss of DT, and after reinduction of DT by an osmotic treatment. To separate proteins induced by the osmotic treatment from those linked with DT, the comparison was extended to 5 mm long emerged radicles for which DT could no longer be reinduced, albeit that drought tolerance was increased. The abundance of 15 polypeptides was linked with DT, out of which 11 were identified as late embryogenesis abundant proteins from different groups: MtEm6 (group 1), one isoform of DHN3 (dehydrins), MtPM25 (group 5), and three members of group 3 (MP2, an isoform of PM18, and all the isoforms of SBP65). In silico analysis revealed that their expression is likely seed specific, except for DHN3. Other isoforms of DNH3 and PM18 as well as three isoforms of the dehydrin Budcar5 were associated with drought tolerance. Changes in the abundance of MtEm6 and MtPM25 in imbibed cotyledons during the loss of DT and in developing embryos during the acquisition of DT confirmed the link of these two proteins with DT. Fourier transform infrared spectroscopy revealed that the recombinant MtPM25 and MtEm6 exhibited a certain degree of order in the hydrated state, but that they became more structured by adopting a helices and b sheets during drying. A model is presented in which DT-linked late embryogenesis abundant proteins might exert different protective functions at high and low hydration levels.

show abstract

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

et al. 2006

View full text Add to dashboard Cite

show abstract

“…The maize full-length tga1 cDNA was cloned into a pVP-GW vector (Singh et al, 2005), which can produce proteins with S-His-tag and enhanced solubility. Proteins were overexpressed in E. coli, and then extracted and purified using Ni-NTA Superflow Columns (Qiagen) following the manufacturer's instructions.…”

Section: Heterologous Protein Expression Andmentioning

confidence: 99%

Evidence That the Origin of Naked Kernels During Maize Domestication Was Caused by a Single Amino Acid Substitution intga1

et al. 2015

View full text Add to dashboard Cite

teosinte glume architecture1 (tga1), a member of the SBP-box gene family of transcriptional regulators, has been identified as the gene conferring naked kernels in maize vs. encased kernels in its wild progenitor, teosinte. However, the identity of the causative polymorphism within tga1 that produces these different phenotypes has remained unknown. Using nucleotide diversity data, we show that there is a single fixed nucleotide difference between maize and teosinte in tga1, and this difference confers a Lys (teosinte allele) to Asn (maize allele) substitution. This substitution transforms TGA1 into a transcriptional repressor. While both alleles of TGA1 can bind a GTAC motif, maize-TGA1 forms more stable dimers than teosinte-TGA1. Since it is the only fixed difference between maize and teosinte, this alteration in protein function likely underlies the differences in maize and teosinte glume architecture. We previously reported a difference in TGA1 protein abundance between maize and teosinte based on relative signal intensity of a Western blot. Here, we show that this signal difference is not due to tga1 but to a second gene, neighbor of tga1 (not1). Not1 encodes a protein that has 92% amino acid similarity to TGA1 and that is recognized by the TGA1 antibody. Genetic mapping and phenotypic data show that tga1, without a contribution from not1, controls the difference in covered vs. naked kernels. No trait differences could be associated with the maize vs. teosinte alleles of not1. Our results document how morphological evolution can be driven by a simple nucleotide change that alters protein function. KEYWORDS tga1; glume architecture; teosinte; maize; domestication A LTHOUGH the study of adaptive evolution through natural or artificial selection dates back to Darwin, the genetic mechanisms that drive changes in morphology remain strongly debated (Stern and Orgogozo 2008). Questions surrounding the number of genes (few or many) and types of mutations (regulatory or coding) in these genes have been a focus in this debate (Carroll 2005(Carroll , 2008Hoekstra and Coyne 2007). These questions can only be answered through the genetic and molecular dissection of genes that have undergone selective pressure between lineages or within populations. Crop species offer a powerful system for investigating these questions since crops are the products of continuous directional selection to adapt them to the human controlled environment and human needs (Meyer and Purugganan 2013). Research on crop models is further facilitated by the extensive genetic and genomic resources available for them. Moreover, because of the recent divergence of crop species from their wild progenitors, crop-progenitor pairs remain cross-compatible and amenable to genetic analysis.Maize was domesticated in the central Balsas valley of Mexico 9000 years ago from a wild relative called teosinte (Piperno et al. 2001;Matsuoka et al. 2002). Because the morphology of modern maize is drastically different from teosinte species, the progenitor of mai...

show abstract

“…Most LEA proteins are hydrophilins, a set of proteins characterized by their biased amino acid composition, richness in Gly and other small and/or charged residues, and high hydrophilicity index (GarayArroyo et al, 2000). This amino acid composition promotes their flexible structure in solution, existing mainly as random coils, with the exception of the hydrophobic or atypical LEA proteins (Singh et al, 2005). Moreover, hydrophilic LEA proteins from groups 2, 3, and 4 show a prevalence of typical spectroscopic patterns of intrinsically unstructured proteins, with the occurrence of transitions from intrinsically unstructured proteins to ordered conformations in the presence of helix-promoting solvents or air drying (McCubbin et al, 1985;Russouw et al, 1995;Eom et al, 1996;Lisse et al, 1996;Ismail et al, 1999;Wolkers et al, 2001;Soulages et al, 2002Soulages et al, , 2003Goyal et al, 2003;Shih et al, 2004;Tolleter et al, 2007).…”

mentioning

confidence: 99%

Functional Analysis of the Group 4 Late Embryogenesis Abundant Proteins Reveals Their Relevance in the Adaptive Response during Water Deficit in Arabidopsis

et al. 2010

View full text Add to dashboard Cite

Late-Embryogenesis Abundant (LEA) proteins accumulate to high levels during the last stages of seed development, when desiccation tolerance is acquired, and in vegetative and reproductive tissues under water deficit, leading to the hypothesis that these proteins play a role in the adaptation of plants to this stress condition. In this work, we obtained the accumulation patterns of the Arabidopsis (Arabidopsis thaliana) group 4 LEA proteins during different developmental stages and plant organs in response to water deficit. We demonstrate that overexpression of a representative member of this group of proteins confers tolerance to severe drought in Arabidopsis plants. Moreover, we show that deficiency of LEA proteins in this group leads to susceptible phenotypes upon water limitation, during germination, or in mature plants after recovery from severe dehydration. Upon recovery from this stress condition, mutant plants showed a reduced number of floral and axillary buds when compared with wild-type plants. The lack of these proteins also correlates with a reduced seed production under optimal irrigation, supporting a role in fruit and/or seed development. A bioinformatic analysis of group 4 LEA proteins from many plant genera showed that there are two subgroups, originated through ancient gene duplication and a subsequent functional specialization. This study represents, to our knowledge, the first genetic evidence showing that one of the LEA protein groups is directly involved in the adaptive response of higher plants to water deficit, and it provides data indicating that the function of these proteins is not redundant to that of the other LEA proteins.

show abstract

Solution structure of a late embryogenesis abundant protein (LEA14) from Arabidopsis thaliana, a cellular stress‐related protein

Cited by 111 publications

References 58 publications

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

Evidence That the Origin of Naked Kernels During Maize Domestication Was Caused by a Single Amino Acid Substitution intga1

Functional Analysis of the Group 4 Late Embryogenesis Abundant Proteins Reveals Their Relevance in the Adaptive Response during Water Deficit in Arabidopsis

Contact Info

Product

Resources

About