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

Copyright © 2013 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 75(2014) vom: 12. Feb., Seite 55-69
1. Verfasser: Edstam, Monika M (VerfasserIn)
Weitere Verfasser: Laurila, Maiju, Höglund, Andrey, Raman, Amitha, Dahlström, Käthe M, Salminen, Tiina A, Edqvist, Johan, Blomqvist, Kristina
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Circular dichroism Cuticle Cutin Heat stability LTP Lipids Moss Carrier Proteins mehr... Fatty Acids, Unsaturated GPI-Linked Proteins Membrane Lipids Plant Proteins lipid transfer protein cutin 54990-88-4 Alanine OF5P57N2ZX
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100 1 |a Edstam, Monika M  |e verfasserin  |4 aut 
245 1 0 |a Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens 
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520 |a Copyright © 2013 Elsevier Masson SAS. All rights reserved. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Circular dichroism 
650 4 |a Cuticle 
650 4 |a Cutin 
650 4 |a Heat stability 
650 4 |a LTP 
650 4 |a Lipids 
650 4 |a Moss 
650 7 |a Carrier Proteins  |2 NLM 
650 7 |a Fatty Acids, Unsaturated  |2 NLM 
650 7 |a GPI-Linked Proteins  |2 NLM 
650 7 |a Membrane Lipids  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a lipid transfer protein  |2 NLM 
650 7 |a cutin  |2 NLM 
650 7 |a 54990-88-4  |2 NLM 
650 7 |a Alanine  |2 NLM 
650 7 |a OF5P57N2ZX  |2 NLM 
700 1 |a Laurila, Maiju  |e verfasserin  |4 aut 
700 1 |a Höglund, Andrey  |e verfasserin  |4 aut 
700 1 |a Raman, Amitha  |e verfasserin  |4 aut 
700 1 |a Dahlström, Käthe M  |e verfasserin  |4 aut 
700 1 |a Salminen, Tiina A  |e verfasserin  |4 aut 
700 1 |a Edqvist, Johan  |e verfasserin  |4 aut 
700 1 |a Blomqvist, Kristina  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 75(2014) vom: 12. Feb., Seite 55-69  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:75  |g year:2014  |g day:12  |g month:02  |g pages:55-69 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2013.12.001  |3 Volltext 
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