Related Experiment Video
Updated: May 18, 2026
Soybean Hairy Root Transformation for the Analysis of Gene Function
Published on: May 5, 2023
Functional studies of soybean (Glycine max L.) seed LEA proteins GmPM6, GmPM11, and GmPM30 by CD and FTIR
Ming-Der Shih1, Tzung-Yang Hsieh, Wei-Ting Jian
1Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan.
Abstract:
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.
