scholarly journals A lipid transfer protein variant with a mutant eight-cysteine motif causes photoperiod- and thermo-sensitive dwarfism in rice

2019 ◽  
Vol 71 (4) ◽  
pp. 1294-1305
Author(s):  
Wenjun Deng ◽  
Riqing Li ◽  
Yiwei Xu ◽  
Runyuan Mao ◽  
Shuifu Chen ◽  
...  

Abstract Plant height is an important trait for architecture patterning and crop yield improvement. Although the pathways involving gibberellins and brassinosteroids have been well studied, there are still many gaps in our knowledge of the networks that control plant height. In this study, we determined that a dominant photoperiod- and thermo-sensitive dwarf mutant is caused by the active role of a mutated gene Photoperiod-thermo-sensitive dwarfism 1 (Ptd1), the wild-type of which encodes a non-specific lipid transfer protein (nsLTP). Ptd1 plants showed severe dwarfism under long-day and low-temperature conditions, but grew almost normal under short-day and high-temperature conditions. These phenotypic variations were associated with Ptd1 mRNA levels and accumulation of the corresponding protein. Furthermore, we found that the growth inhibition in Ptd1 may result from the particular protein conformation of Ptd1 due to loss of two disulfide bonds in the eight-cysteine motif (8-CM) that is conserved among nsLTPs. These results contribute to our understanding of the novel function of disulfide bonds in the 8-CM, and provide a potential new strategy for regulation of cell development and plant height by modifying the amino acid residues involved in protein conformation patterning.

2020 ◽  
Vol 71 (4) ◽  
pp. 1203-1205 ◽  
Author(s):  
Li Zhu ◽  
Qian Qian

This article comments on: Deng WJ, Li RQ, Xu YW, Mao RY, Chen SF, Chen LB, Chen LT, Liu YG, Chen YL. 2020. A lipid transfer protein variant with a mutant eight-cysteine motif causes photoperiod- and temperature-sensitive dwarfism in rice. Journal of Experimental Botany 71, 1294–1305.


Acta Naturae ◽  
2015 ◽  
Vol 7 (3) ◽  
pp. 65-73 ◽  
Author(s):  
I. V. Bogdanov ◽  
E. I. Finkina ◽  
S. V. Balandin ◽  
D. N. Melnikova ◽  
E. A. Stukacheva ◽  
...  

The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the -helical structure. It was found that Lc-LTP1 and Lc-LTP3 possess antimicrobial activity and can bind fatty acids. Both isoforms have the ability to bind specific IgE from sera of patients with food allergies, which recognize similar epitopes of the major peach allergen Pru p 3. Both isoforms were shown to have immunological properties similar to those of other plant allergenic LTPs, but Lc-LTP3 displayed a less pronounced immunoreactivity.


Author(s):  
Zulema Gonzalez-Klein ◽  
Bruno Cuevas-Zuviria ◽  
Andrea Wangorsch ◽  
Guadalupe Hernandez-Ramirez ◽  
Diego Pazos-Castro ◽  
...  

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.


2010 ◽  
Vol 58 (10) ◽  
pp. 6490-6497 ◽  
Author(s):  
Bernadett Berecz ◽  
E. N. Clare Mills ◽  
László Tamás ◽  
Ferenc Láng ◽  
Peter R. Shewry ◽  
...  

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