Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 401242
Title Characterization of Two Soybean (Clycine max. L) LEA IV Proteins by Circular Dichroism and Fourier Transform Infrared Spectrometry
Author(s) Shih, M.D.; Hsieh, T.Y.; Lin, T.P.; Hsing, Y.I.; Hoekstra, F.A.
Source Plant and Cell Physiology 51 (2010)3. - ISSN 0032-0781 - p. 395 - 407.
DOI https://doi.org/10.1093/pcp/pcq005
Department(s) Laboratory of Plant Physiology
EPS
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) embryogenesis-abundant protein - desiccation tolerance - arabidopsis-thaliana - nucleotide-sequence - secondary structure - plant desiccation - abscisic-acid - alpha-helix - dry state - gene
Abstract Late embryogenesis-abundant (LEA) proteins, accumulating to a high level during the late stages of seed development, may play a role as osmoprotectants. However, the functions and mechanisms of LEA proteins remained to be elucidated. Five major groups of LEA proteins have been described. In the present study, we report on the characterization of two members of soybean LEA IV proteins, basic GmPM1 and acidic GmPM28, by circular dichroism and Fourier transform infrared spectroscopy. The spectra of both proteins revealed limited defined secondary structures in the fully hydrated state. Thus, the soybean LEA IV proteins are members of ‘natively unfolded proteins’. GmPM1 or GmPM28 proteins showed a conformational change under hydrophobic or dry conditions. After fast or slow drying, the two proteins showed slightly increased proportions of defined secondary structures (a-helix and ß-sheet), from 30 to 49% and from 34 to 42% for GmPM1 and GmPm28, respectively. In the dehydrated state, GmPM1 and GmPM28 interact with non-reducing sugars to improve the transition temperature of cellular glass, with poly-l-lysine to prevent dehydration-induced aggregation and with phospholipids to maintain the liquid crystal phase over a wide temperature range. Our work suggests that soybean LEA IV proteins are functional in the dry state. They are one of the important components in cellular glasses and may stabilize desiccation-sensitive proteins and plasma membranes during dehydration
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