scholarly journals OsmiR535, a Potential Genetic Editing Target for Drought and Salinity Stress Tolerance in Oryza sativa

Plants ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1337
Author(s):  
Erkui Yue ◽  
Huan Cao ◽  
Bohan Liu
Keyword(s):  
Oryza Sativa ◽  
Stress Response ◽  
Molecular Breeding ◽  
Mirna Family ◽  
Plant Responses ◽  
Practical Application ◽  
Poly Ethylene Glycol ◽  
Poly Ethylene ◽  
Post Stress

OsmiR535 belongs to the miR156/miR529/miR535 superfamily, a highly conserved miRNA family in plants. OsmiR535 is involved in regulating the cold-stress response, modulating plant development, and determining panicle architecture and grain length. However, the role that OsmiR535 plays in plant responses to drought and salinity are elusive. In the current study, molecular and genetic engineering techniques were used to elucidate the possible role of OsmiR535 in response to NaCl, PEG(Poly ethylene glycol), ABA(Abscisic acid), and dehydration stresses. Our results showed that OsmiR535 is induced under stressed conditions as compared to control. With transgenic and CRISPR/Cas9 knockout system techniques, our results verified that either inhibition or knockout of OsmiR535 in rice could enhance the tolerance of plants to NaCl, ABA, dehydration and PEG stresses. In addition, the overexpression of OsmiR535 significantly reduced the survival rate of rice seedlings during PEG and dehydration post-stress recovery. Our results demonstrated that OsmiR535 negatively regulates the stress response in rice. Moreover, our practical application of CRISPR/Cas9 mediated genome editing created a homozygous 5 bp deletion in the coding sequence of OsmiR535, demonstrating that OsmiR535 could be a useful genetic editing target for drought and salinity tolerance and a new marker for molecular breeding of Oryza sativa.

The role of hydrogen bonding in alginate/poly(acrylamide-co-dimethylacrylamide) and alginate/poly(ethylene glycol) methyl ether methacrylate-based tough hybrid hydrogels

RSC Advances ◽  
2015 ◽  
Vol 5 (71) ◽  
pp. 57678-57685 ◽  
Author(s):  
Zhi Wei Low ◽  
Pei Lin Chee ◽  
Dan Kai ◽  
Xian Jun Loh
Keyword(s):  
Hydrogen Bonding ◽  
Elastic Modulus ◽  
Ethylene Glycol ◽  
Methyl Ether ◽  
Poly Ethylene Glycol ◽  
Hybrid Hydrogels ◽  
Poly Ethylene ◽  
Glycol Methyl Ether ◽  
Poly Acrylamide

Hybrid hydrogels, with an elastic modulus and compressive toughness of 350 kPa and 70 J m−3, was synthesized and reported here.

Investigation of the role of hydrophilic chain length in amphiphilic perfluoropolyether/poly(ethylene glycol) networks: towards high-performance antifouling coatings

Biofouling ◽  
2011 ◽  
Vol 27 (10) ◽  
pp. 1139-1150 ◽  
Author(s):  
Yapei Wang ◽  
Louis M. Pitet ◽  
John A. Finlay ◽  
Lenora H. Brewer ◽  
Gemma Cone ◽  
...  
Keyword(s):  
Ethylene Glycol ◽  
Chain Length ◽  
High Performance ◽  
Poly Ethylene Glycol ◽  
Antifouling Coatings ◽  
Poly Ethylene

scholarly journals Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues

1997 ◽  
Vol 325 (3) ◽  
pp. 685-691 ◽  
Author(s):  
Desong CHEN ◽  
R. Manjunatha KINI ◽  
Raymond YUEN ◽  
Hoon Eng KHOO
Keyword(s):  
Cell Membrane ◽  
Ethylene Glycol ◽  
Haemolytic Activity ◽  
Side Chains ◽  
Poly Ethylene Glycol ◽  
Arginine Residues ◽  
Poly Ethylene ◽  
Cationic Residues ◽  
Positively Charged

Stonustoxin (SNTX) is a two-subunit protein toxin purified from the venom of the stonefish (Synanceja horrida), which induces potent haemolytic activity. We examined the pore-forming property of this non-enzymic protein by an osmotic protection assay. SNTX-induced haemolysis was completely prevented by osmotic protectants of adequate size [poly(ethylene) glycol 3000; molecular diameter approx. 3.2 nm]. Uncharged molecules of smaller size, such as raffinose and poly(ethylene) glycol 1000–2000, failed to protect against cell lysis. These findings indicate that SNTX induces the formation of hydrophilic pores in the cell membrane, which results in the lysis of erythrocytes. Since cationic residues contribute significantly to the cytolytic activity of several other pore-forming toxins, we examined the role of positively charged lysine and arginine residues in the haemolytic activity of SNTX. SNTX lost its haemolytic activity when the positively charged side chains of lysine residues were neutralized or converted into negatively charged side chains upon carbamylation or succinylation respectively. The haemolytic activity of SNTX was also inhibited by the modification of positively charged arginine residues using 2,3-butanedione. The loss of haemolysis showed strong correlation with the number of Lys or Arg residues modified. CD analyses, however, showed that the conformation of SNTX was not significantly affected by these chemical modifications. Further, the haemolytic activity of SNTX was competitively inhibited by various negatively charged lipids, such as phosphatidylserine, cardiolipin and monosialogangliosides. These results indicate that SNTX induces potent haemolytic activity through the formation of pores in the cell membrane, and that cationic residues play a crucial role in its cytolytic mechanism.

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