Characterization of GPI-anchored lipid transfer proteins in Physcomitrella patens

• Published in: Plant physiology and biochemistry 2014, Vol.75, p.55
• Main Authors: Edstam, Monika M., Laurila, Maiju, Höglund, Andrey, Raman, Amitha, Dahlström, Käthe M., Salminen, Tiina A., Edqvist, Johan, Blomqvist, Kristina
• Format: Article
• Language: English
• ISSN: 0981-9428; 1873-2690
• DOI: 10.1016/j.plaphy.2013.12.001

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. Physcomitrella 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. Expression of a moss LTPG-YFP fusion revealed localization to the plasma membrane. The expression of many of the moss LTPGs were found to be upregulated during drought and cold treatments. Lipid profiling revealed that cutin monomers, such as C16 and C18 mono- and di-hydroxylated fatty acids, could be identified in Physcomitrella.