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

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: Monika M. Edstam, Maiju Laurila, Andrey Höglund, Amitha Raman, Käthe M. Dahlström, Tiina A. Salminen, Johan Edqvist, Kristina Blomqvist
Publiceringsår: 2014
Tidskrift: Plant Physiology and Biochemistry
Tidskriftsakronym: PLANT PHYSIOL BIOCH
Volym: 75
Artikelns första sida, sidnummer: 55
Artikelns sista sida, sidnummer: 69
Antal sidor: 15
ISSN: 0981-9428
eISSN: 1873-2690


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.


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


Senast uppdaterad 2020-01-06 vid 02:32