scholarly journals Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase

Nature ◽  
2014 ◽  
Vol 518 (7537) ◽  
pp. 120-124 ◽  
Author(s):  
Timothy H. Tran ◽  
Yu-Shan Hsiao ◽  
Jeanyoung Jo ◽  
Chi-Yuan Chou ◽  
Lars E. P. Dietrich ◽  
...  
2020 ◽  
Vol 131 (1-2) ◽  
pp. 83-89 ◽  
Author(s):  
Megan E. Beck ◽  
Yuxun Zhang ◽  
Sivakama S. Bharathi ◽  
Beata Kosmider ◽  
Karim Bahmed ◽  
...  

OCL ◽  
2015 ◽  
Vol 23 (1) ◽  
pp. D113 ◽  
Author(s):  
Blake R. Hopiavuori ◽  
Lea D. Bennett ◽  
Richard S. Brush ◽  
Matthew J. Van Hook ◽  
Wallace B. Thoreson ◽  
...  

Plants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 262 ◽  
Author(s):  
Li-Juan Xie ◽  
Wei-Juan Tan ◽  
Yi-Cong Yang ◽  
Yi-Fang Tan ◽  
Ying Zhou ◽  
...  

In Arabidopsis thaliana, LONG-CHAIN ACYL-COA SYNTHETASEs (LACSs) catalyze the synthesis of long-chain acyl-CoAs and function in diverse biological processes. We have recently revealed that LACS2 is primarily involved in the production of polyunsaturated linolenoyl-CoA, essential for the activation of ethylene response transcription factors-mediated hypoxia signaling. Here, we further reported the dual role of LACS2 in the regulation of submergence tolerance by modulating cuticle permeability in Arabidopsis cells. LACS2-overexpressors (LACS2-OEs) showed improved tolerance to submergence, with higher accumulation of cuticular wax and cutin in their rosettes. In contrast, knockout of LACS2 in the lacs2-3 mutant resulted in hypersensitivity to submergence with reduced wax crystals and thinner cutin layer. By analyses of plant surface permeability, we observed that the hypoxic sensitivities in the LACS2-OEs and lacs2-3 mutant were physiologically correlated with chlorophyll leaching, water loss rates, ionic leakage, and gas exchange. Thus, our findings suggest the role of LACS2 in plant response to submergence by modulating cuticle permeability in plant cells.


1968 ◽  
Vol 22 ◽  
pp. 1361-1363 ◽  
Author(s):  
Karl-Anders Karlsson ◽  
Bo E. Samuelsson ◽  
Göran O. Steen ◽  
Ulrich Schwieter ◽  
Jaakko Paasivirta

2020 ◽  
Vol 5 (22) ◽  
pp. 6594-6607
Author(s):  
Yoshinori Abiko ◽  
Takuto Hayasaki ◽  
Shuhei Hirayama ◽  
Ahmed A. Almarasy ◽  
Youhei Kawabata ◽  
...  

2016 ◽  
Vol 30 ◽  
pp. 177-188 ◽  
Author(s):  
Ilse A.C. Arnoldussen ◽  
Valerio Zerbi ◽  
Maximilian Wiesmann ◽  
Rikko H.J. Noordman ◽  
Simone Bolijn ◽  
...  

Life ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 236
Author(s):  
Masoud Delfi ◽  
Alessandro Emendato ◽  
Serena Leone ◽  
Eros Antonio Lampitella ◽  
Piero Porcaro ◽  
...  

Sweet proteins are a class of proteins with the ability to elicit a sweet sensation in humans upon interaction with sweet taste receptor T1R2/T1R3. Single-chain Monellin, MNEI, is among the sweetest proteins known and it could replace sugar in many food and beverage recipes. Nonetheless, its use is limited by low stability and high aggregation propensity at neutral pH. To solve this inconvenience, we designed a new construct of MNEI, dubbed Mut9, which led to gains in both sweetness and stability. Mut9 showed an extraordinary stability in acidic and neutral environments, where we observed a melting temperature over 20 °C higher than that of MNEI. In addition, Mut9 resulted twice as sweet than MNEI. Both proteins were extensively characterized by biophysical and sensory analyses. Notably, Mut9 preserved its structure and function even after 10 min boiling, with the greatest differences being observed at pH 6.8, where it remained folded and sweet, whereas MNEI lost its structure and function. Finally, we performed a 6-month shelf-life assessment, and the data confirmed the greater stability of the new construct in a wide range of conditions. These data prove that Mut9 has an even greater potential for food and beverage applications than MNEI.


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