Influence of drying on the secondary structure of intrinsically disordered and globular proteins

Hundertmark, Michaela; Popova, Antoaneta V.; Rausch, Saskia; Seckler, Robert; Hincha, Dirk K.

doi:10.1016/j.bbrc.2011.11.067

Cited by 39 publications

(46 citation statements)

References 42 publications

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“…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%

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

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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.

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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

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“…7). Again, these modest degrees of water stress are unlikely to promote substantial coiling of LEA proteins as judged by several in vitro models (Furuki et al, 2011;Hundertmark et al, 2012;Li and He, 2009;Popova et al, 2011). Thus AfLEA1.3 may interact in some fashion with proteins or membranes in the uncoiled state.…”

Section: Discussionmentioning

confidence: 99%

Improved tolerance to salt and water stress in Drosophila melanogaster cells conferred by late embryogenesis abundant protein

Marunde

Samarajeewa

Anderson

et al. 2013

Journal of Insect Physiology

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Graphical AbstractHighlights: ØThe Late Embryogenesis Abundant protein AfLEA1.3 from Artemia franciscana accumulates in the mitochondrion of Drosophila Kc167 cells. Ø AfLEA1.3 improves mitochondrial functions in presence of high sodium chloride concentrations. Ø AfLEA1.3 reduces mitochondrial damage during freeze-thawing. Ø AfLEA1.3 increases cellular tolerance to osmotic stress. Ø AfLEA1.3 increases cellular tolerance to convective drying.

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“…LEA proteins, often enriched in repeated motifs, are hydrophilic, mostly unstructured, flexible proteins within the group of intrinsically disordered proteins; however, when drying, many LEA proteins reversibly assume structure stabilized by hydrogen bonding and electrostatic interactions (Goyal et al 2003;Chakrabortee et al 2011;Hundertmark et al 2012;Hatanaka et al 2013). LEA proteins were first discovered in maturing plant seeds (Dure et al 1981) and have since been found in desiccation-tolerant cyanobacter (Close and Lammers 1993), bacteria and Archaea (Campos et al 2013), nematodes (Browne et al 2002;Gal et al 2004;Goyal et al 2005a;Erkut et al 2013), rotifers (Tunnacliffe et al 2005), an insect (Kikawada et al 2006;Hatanaka et al 2013), and a crustacean (Hand et al 2007;Sharon et al 2009).…”

Section: Lea Proteins and Desiccation Tolerance In Artemia Cystsmentioning

confidence: 99%

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

MacRae

2016

Cell Stress and Chaperones

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Oviparously developing embryos of the brine shrimp, Artemia, arrest at gastrulation and are released from females as cysts before entering diapause, a state of dormancy and stress tolerance. Diapause is terminated by an external signal, and growth resumes if conditions are permissible. However, if circumstances are unfavorable, cysts enter quiescence, a dormant stage that continues as long as adverse conditions persist. Artemia embryos in diapause and quiescence are remarkably resistant to environmental and physiological stressors, withstanding desiccation, cold, heat, oxidation, ultraviolet radiation, and years of anoxia at ambient temperature when fully hydrated. Cysts have adapted to stress in several ways; they are surrounded by a rigid cell wall impermeable to most chemical compounds and which functions as a shield against ultraviolet radiation. Artemia cysts contain large amounts of trehalose, a non-reducing sugar thought to preserve membranes and proteins during desiccation by replacing water molecules and/or contributing to vitrification. Late embryogenesis abundant proteins similar to those in seeds and other anhydrobiotic organisms are found in cysts, and they safeguard cell organelles and proteins during desiccation. Artemia cysts contain abundant amounts of p26, a small heat shock protein, and artemin, a ferritin homologue, both ATPindependent molecular chaperones important in stress tolerance. The evidence provided in this review supports the conclusion that it is the interplay of these protective elements that make Artemia one of the most stress tolerant of all metazoan organisms.

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Influence of drying on the secondary structure of intrinsically disordered and globular proteins

Cited by 39 publications

References 42 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

Improved tolerance to salt and water stress in Drosophila melanogaster cells conferred by late embryogenesis abundant protein

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

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