Seed Proteins 1999
DOI: 10.1007/978-94-011-4431-5_32
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LEA Proteins

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Cited by 138 publications
(179 citation statements)
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“…They are listed in Table IV. The majority of these proteins corresponded to proteins normally synthesized during seed development, such as 12S globulin subunits and members of the dehydrin family (group 2 late embryogenesis abundant [LEA] proteins; Finkelstein, 1993;Bewley and Black, 1994;Cuming, 1999). In other words, it seemed that transcriptional inhibition by a-amanitin somehow allowed the germinating seeds to recapitulate part of the maturation program, by favoring the use of stored mRNAs encoding maturation proteins.…”
Section: De Novo Protein Patternsmentioning
confidence: 99%
“…They are listed in Table IV. The majority of these proteins corresponded to proteins normally synthesized during seed development, such as 12S globulin subunits and members of the dehydrin family (group 2 late embryogenesis abundant [LEA] proteins; Finkelstein, 1993;Bewley and Black, 1994;Cuming, 1999). In other words, it seemed that transcriptional inhibition by a-amanitin somehow allowed the germinating seeds to recapitulate part of the maturation program, by favoring the use of stored mRNAs encoding maturation proteins.…”
Section: De Novo Protein Patternsmentioning
confidence: 99%
“…LEA1) possibly serve as water-binding domains, act as hydration buffer to regulate water status, or may also interact with the surface of macromolecules as a water matrix to oppose protein denaturation in the dehydrating tissues thereby solvating the cytosolic structures (McCubbin et al, 1985;Baker et al, 1988;Dure, 1993;Cuming, 1999). The charged amino acid motifs in LEA3 may aid in sequestering ions that accumulate under water deficit conditions (Dure, 1993).…”
Section: Lea Proteinsmentioning
confidence: 99%
“…Based on sequence similarity and amino acid representation, LEA proteins have been assigned to various families and groups, but the mechanisms by which cellular protection is conferred under water stress are still poorly understood (Battaglia et al, 2008;Cuming, 1999;Tunnacliffe and Wise, 2007;Wise and Tunnacliffe, 2004). Interaction with phospholipids was reported for COR15am, a group 3 LEA protein, which was shown to interact with membranes during phase transition to the frozen state in Arabidopsis thaliana (Steponkus et al, 1998), and reports suggest that gaining secondary structure during desiccation may contribute to the ability of LEA proteins to stabilize proteins, membranes, and sugar glasses during drying (Furuki et al, 2011;Li and He, 2009;).…”
Section: Introductionmentioning
confidence: 99%