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

Plant Sci. 2012 Nov:196:152-9. doi: 10.1016/j.plantsci.2012.07.012. Epub 2012 Aug 20.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism / methods*
  • Desiccation
  • Electrophoresis, Polyacrylamide Gel
  • Glycine max / genetics
  • Glycine max / metabolism*
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Phospholipids / chemistry
  • Phospholipids / metabolism
  • Polylysine / chemistry
  • Polylysine / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Soybean Proteins / chemistry*
  • Soybean Proteins / genetics
  • Soybean Proteins / metabolism*
  • Spectroscopy, Fourier Transform Infrared / methods*
  • Sucrose / chemistry
  • Sucrose / metabolism

Substances

  • Molecular Chaperones
  • Phospholipids
  • Recombinant Proteins
  • Soybean Proteins
  • Polylysine
  • Sucrose