Functional studies of soybean (Glycine max L.) seed LEA proteins GmPM6, GmPM11, and GmPM30 by CD and FTIR spectroscopy

The protein and mRNA levels of late embryogenesis abundant (LEA) genes may be linked to osmotic stresses. Here, we characterized three soybean hydrophilic LEA proteins – GmPM11 (LEA I), GmPM6 (LEA II), and GmPM30 (LEA III) – by circular dichroism and Fourier transform infrared spectroscopy. Structur...

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Veröffentlicht in:	Plant science (Limerick) 2012-11, Vol.196, p.152-159
Hauptverfasser:	Shih, Ming-Der, Hsieh, Tzung-Yang, Jian, Wei-Ting, Wu, Ming-Tsung, Yang, Shin-Jin, Hoekstra, Folkert A, Hsing, Yue-Ie C
Format:	Artikel
Sprache:	eng
Schlagworte:	arabidopsis-thaliana Biological and medical sciences Circular dichroism Circular Dichroism - methods dehydration Desiccation Desiccation tolerance drying Electrophoresis, Polyacrylamide Gel embryogenesis-abundant protein expression Fourier transform infrared spectroscopy Fundamental and applied biological sciences. Psychology genes Glycine max Glycine max - genetics Glycine max - metabolism Glycine max physiologically mature proteins Hydrophobic and Hydrophilic Interactions hydrophobicity Late embryogenesis abundant messenger RNA Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism nonreducing sugars osmotic stress Phospholipids - chemistry Phospholipids - metabolism plants Polylysine - chemistry Polylysine - metabolism Protein Binding Protein Conformation Protein Structure, Secondary proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism saccharomyces-cerevisiae secondary structure seeds Soybean Soybean Proteins - chemistry Soybean Proteins - genetics Soybean Proteins - metabolism soybeans Spectroscopy, Fourier Transform Infrared - methods Sucrose - chemistry Sucrose - metabolism wheat-germ
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Zusammenfassung:	The protein and mRNA levels of late embryogenesis abundant (LEA) genes may be linked to osmotic stresses. Here, we characterized three soybean hydrophilic LEA proteins – GmPM11 (LEA I), GmPM6 (LEA II), and GmPM30 (LEA III) – by circular dichroism and Fourier transform infrared spectroscopy. Structural analysis revealed that the LEA proteins adopted high amounts of disordered conformations in solution and underwent conformational changes with hydrophobicity and desiccation induction. Macromolecular interaction studies revealed that the GmPM proteins interact with non-reducing sugars and phospholipids. GmPM6 and GmPM30 but not GmPM11 could prevent beta-aggregation of poly-l-lysine after slow drying. We discuss the possible functions of hydrophilic LEA proteins in maturing seeds.
ISSN:	0168-9452 1873-2259
DOI:	10.1016/j.plantsci.2012.07.012