Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens

Monika M. Edstam, Maiju Laurila, Andrey Höglund, Amitha Raman, Käthe Dahlström, Tiina Salminen, Johan Edqvist, Kristina Blomqvist

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The non-specific lipid transfer proteins (nsLTPs) are characterized by a compact structure with a central hydrophobic cavity very suitable for binding hydrophobic ligands, such as lipids. The nsLTPs are encoded by large gene families in all land plant lineages, but seem to be absent from green algae. The nsLTPs are classified to different types based on molecular weight, sequence similarity, intron position or spacing between the cysteine residues. The Type G nsLTPs (LTPGs) have a GPI-anchor in the C-terminal region which may attach the protein to the exterior side of the plasma membrane. Here, we present the first characterization of nsLTPs from an early diverged plant, the moss Physcomitrella patens. Moss LTPGs were heterologously produced and purified from Pichia pastoris. The purified moss LTPGs were found to be extremely heat stable and showed a binding preference for unsaturated fatty acids. Structural modeling implied that high alanine content could be important for the heat stability. Lipid profiling revealed that cutin monomers, such as C-16 and C-18 mono- and di-hydroxylated fatty acids, could be identified in P. patens. Expression of a moss LTPG-YFP fusion revealed localization to the plasma membrane. The expressions of many of the moss LTPGs were found to be upregulated during drought and cold treatments.
Original languageUndefined/Unknown
Pages (from-to)55–69
Number of pages15
JournalPlant Physiology and Biochemistry
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed


  • Circular dichroism
  • Cuticle
  • Cutin
  • Heat stability
  • Lipids
  • LTP
  • Moss

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