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

Copyright © 2013 Elsevier Masson SAS. All rights reserved.

Détails bibliographiques
Publié dans:Plant physiology and biochemistry : PPB. - 1991. - 75(2014) vom: 12. Feb., Seite 55-69
Auteur principal: Edstam, Monika M (Auteur)
Autres auteurs: Laurila, Maiju, Höglund, Andrey, Raman, Amitha, Dahlström, Käthe M, Salminen, Tiina A, Edqvist, Johan, Blomqvist, Kristina
Format: Article en ligne
Langue:English
Publié: 2014
Accès à la collection:Plant physiology and biochemistry : PPB
Sujets:Journal Article Research Support, Non-U.S. Gov't Circular dichroism Cuticle Cutin Heat stability LTP Lipids Moss Carrier Proteins plus... Fatty Acids, Unsaturated GPI-Linked Proteins Membrane Lipids Plant Proteins lipid transfer protein cutin 54990-88-4 Alanine OF5P57N2ZX
Description
Résumé:Copyright © 2013 Elsevier Masson SAS. All rights reserved.
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 C16 and C18 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
Description:Date Completed 29.09.2014
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2013.12.001