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

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Monika M. Edstam, Maiju Laurila, Andrey Höglund, Amitha Raman, Käthe M. Dahlström, Tiina A. Salminen, Johan Edqvist, Kristina Blomqvist
Publisher: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Publication year: 2014
Journal: Plant Physiology and Biochemistry
Journal acronym: PLANT PHYSIOL BIOCH
Volume number: 75
Start page: 55
End page: 69
Number of pages: 15
ISSN: 0981-9428
eISSN: 1873-2690


Abstract

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.


Keywords

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


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