scholarly journals Water Relations and Low-Temperature Acclimation for Cactus Species Varying in Freezing Tolerance

1994 ◽  
Vol 104 (2) ◽  
pp. 675-681 ◽  
Author(s):  
G. Goldstein ◽  
P. S. Nobel
1977 ◽  
Vol 69 (1) ◽  
pp. 13-21
Author(s):  
DENNIS J. MURPHY

1. A time course of the changes in blood Ca2+ and freezing tolerance of Modiolus demissus (Dillwyn) demonstrated that increases in freezing tolerance parallel increases in blood Ca2+. The increases in freezing tolerance occurred rapidly, suggesting that Ca2+ affects freezing tolerance directly by its presence in the blood. 2. The presence of La3+ reduced the freezing tolerance of isolated foot muscle. Thus, Ca2+ appears to increase freezing tolerance directly by binding to cell membranes. 3. The loss of the contractile response of freeze-thawed foot muscle to Ach, KCl and caffeine and the continued response to CaCl2 suggested that cell membranes are the primary sites of freezing injury. 4. The increase in blood Ca2+ following low-temperature acclimation accounted for only 40% of the total change in freezing tolerance. Therefore, other mechanisms responsible for increasing the freezing tolerance of M. demissus following low temperature acclimation also exist.


1977 ◽  
Vol 69 (1) ◽  
pp. 1-12
Author(s):  
DENNIS J. MURPHY

1. A physiological mechanism responsible for increasing the freezing tolerance of the bivalve Modiolus demissus (Dillwyn) following low-temperature acclimation was demonstrated. 2. The rates of oxygen consumption of M. demissus acclimated to temperatures between 0 and 24 °C were presented as an Arrhenius plot. A change in slope occurred at 10 °C, suggesting that temperature alone was not responsible for the increased decline in the rate of oxygen consumption below 10 °C. 3. Low-temperature acclimation had no effect on blood Na+ or K+ concentrations but did reduce the concentration of blood Mg2+ and, in addition, resulted in the accumulation of end-products characteristic of anaerobic metabolism - tissue alanine and proline, and blood Ca2+. Furthermore, maintenance of M. demissus under anaerobic conditions increased freezing tolerance. 4. Taken together, these data indicate that the increased freezing tolerance of M. demissus acclimated to low temperatures involves a conversion to anaerobic metabolism. 5. The increase in blood Ca2+ following low-temperature acclimation was associated with the increased freezing tolerance. Finally, Mg2+ simulated the effect of Ca2+ on freezing tolerance, but was only 20% as effective. 6. These results suggest that a Ca2+-dependent mechanism responsible for increasing the freezing tolerance of M. demissus exists, and that the increase in blood Ca2+ is due to a conversion to anaerobic metabolism.


2016 ◽  
Vol 100 ◽  
pp. 157-168 ◽  
Author(s):  
Bin Liang ◽  
Deyong Kong ◽  
Jincai Ma ◽  
Chongqing Wen ◽  
Tong Yuan ◽  
...  

1998 ◽  
Vol 152 (4-5) ◽  
pp. 473-479 ◽  
Author(s):  
Alexey I. Zabotin ◽  
Tatyana S. Barisheva ◽  
Olga A. Zabotina ◽  
Irina A. Larskaya ◽  
Vera V. Lozovaya ◽  
...  

Phyton ◽  
2022 ◽  
Vol 91 (3) ◽  
pp. 583-598
Author(s):  
Muslum S. Inal ◽  
Dilek Unal ◽  
Bengu Turkyilmaz Unal ◽  
Munir Ozturk

2020 ◽  
Vol 67 (4) ◽  
pp. 758-766
Author(s):  
M. Bahmani ◽  
R. Maali-Amiri ◽  
M. Javan-Nikkhah ◽  
O. Atghia ◽  
A. Rasolnia

2019 ◽  
Vol 60 (12) ◽  
pp. 2744-2757 ◽  
Author(s):  
Sung Mi Cho ◽  
Sanghee Kim ◽  
Hojin Cho ◽  
Hyoungseok Lee ◽  
Jun Hyuck Lee ◽  
...  

Abstract Microalgal ice-binding proteins (IBPs) in the polar region are poorly understood at the genome-wide level, although they are important for cold adaptation. Through the transcriptome study with the Arctic green alga Chloromonas sp. KNF0032, we identified six Chloromonas IBP genes (CmIBPs), homologous with the previously reported IBPs from Antarctic snow alga CCMP681 and Antarctic Chloromonas sp. They were organized with multiple exon/intron structures and low-temperature-responsive cis-elements in their promoters and abundantly expressed at low temperature. The biological functions of three representative CmIBPs (CmIBP1, CmIBP2 and CmIBP3) were tested using in vitro analysis and transgenic plant system. CmIBP1 had the most effective ice recrystallization inhibition (IRI) activities in both in vitro and transgenic plants, and CmIBP2 and CmIBP3 had followed. All transgenic plants grown under nonacclimated condition were freezing tolerant, and especially 35S::CmIBP1 plants were most effective. After cold acclimation, only 35S::CmIBP2 plants showed slightly increased freezing tolerance. Structurally, the CmIBPs were predicted to have β-solenoid forms with parallel β-sheets and repeated TXT motifs. The repeated TXT structure of CmIBPs appears similar to the AidA domain-containing adhesin-like proteins from methanogens. We have shown that the AidA domain has IRI activity as CmIBPs and phylogenetic analysis also supported that the AidA domains are monophyletic with ice-binding domain of CmIBPs, and these results suggest that CmIBPs are a type of modified adhesins.


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