scholarly journals Cryoprotectin: a plant lipid–transfer protein homologue that stabilizes membranes during freezing

2002 ◽  
Vol 357 (1423) ◽  
pp. 909-916 ◽  
Author(s):  
Dirk K. Hincha

Plants from temperate and cold climates are able to increase their freezing tolerance during exposure to low non–freezing temperatures. It has been shown that several genes are induced in a coordinated manner during this process of cold acclimation. The functional role of most of the corresponding cold–regulated proteins is not yet known. We summarize our knowledge of those cold–regulated proteins that are able to stabilize membranes during a freeze–thaw cycle. Special emphasis is placed on cryoprotectin, a lipid–transfer protein homologue that was isolated from cold–acclimated cabbage leaves and that protects isolated chloroplast thylakoid membranes from freeze–thaw damage.

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  

(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.


2006 ◽  
Vol 281 (51) ◽  
pp. 38981-38988 ◽  
Author(s):  
Bénédicte Bakan ◽  
Mats Hamberg ◽  
Ludivine Perrocheau ◽  
Daniel Maume ◽  
Hélène Rogniaux ◽  
...  

2013 ◽  
Vol 357-360 ◽  
pp. 939-943 ◽  
Author(s):  
Jian Gang Niu ◽  
Liang Yan ◽  
Hai Tao Zhai

Based on the coupling testing program of freeze-thaw and carbonation, the laboratory simulation test is carried out. The laws of carbonation depth of the fly ash concrete suffered the freeze-thaw cycle in different test modes and the influence of fly ash dosage on concrete carbonation depth after the freeze-thaw cycle are studied. Defining the influence coefficient of the freeze-thaw cycles on carbonation depth of concrete, the mechanism of coupling of freeze-thaw and carbonation is analyzed,and the role of freeze-thaw and carbonation in the coupling process are obtained.


Membranes ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 357
Author(s):  
Daria Melnikova ◽  
Ivan Bogdanov ◽  
Tatiana Ovchinnikova ◽  
Ekaterina Finkina

It is known that plant lipid transfer proteins (LTPs) bind a broad spectrum of ligands including fatty acids (FAs), phospho- and glycolipids, acyl-coenzyme A and secondary metabolites. In this work, we used protein−lipid overlay assays to identify new putative LTP ligands. In our experiments, the lentil lipid transfer protein Lc-LTP2 as well as LTPs from other plants were shown to bind phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2). Molecular modeling, 2-p-toluidinonaphthalene-6-sulphonate (TNS) displacement and liposome leakage experiments with Lc-LTP2 and its mutant analogs (R45A, Y80A, R45A/Y80A) were performed to investigate interactions between the protein and PI(4,5)P2. It was shown that PI(4,5)P2 initially interacted with the “bottom” entrance of the protein cavity and after complex formation the large polar head of this ligand was also oriented towards the same entrance. We also found that two highly conserved residues in plant LTPs, Arg45 and Tyr80, played an important role in protein-ligand interactions. Apparently, Arg45 is a key residue for interaction with PI(4,5)P2 during both initial contacting and holding in the protein cavity, while Tyr80 is probably a key amino acid playing an essential role in Lc-LTP2 docking to the membrane. Thus, we assumed that the ability of Lc-LTP2 to bind PI(4,5)P2 suggests the involvement of this protein in plant signal transduction.


2010 ◽  
Vol 152 (2) ◽  
pp. 178-183 ◽  
Author(s):  
Arantxa Palacin ◽  
Joan Bartra ◽  
Rosa Muñoz ◽  
Araceli Diaz-Perales ◽  
Antonio Valero ◽  
...  

2011 ◽  
Vol 156 (3) ◽  
pp. 291-296 ◽  
Author(s):  
Leticia Tordesillas ◽  
Sofía Sirvent ◽  
Araceli Díaz-Perales ◽  
Mayte Villalba ◽  
Javier Cuesta-Herranz ◽  
...  

1998 ◽  
Vol 257 (2) ◽  
pp. 443-448 ◽  
Author(s):  
Alain Zachowski ◽  
Francoise Guerbette ◽  
Michele Grosbois ◽  
Alain Jolliot-Croquin ◽  
Jean-Claude Kader

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