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1.
Methods Cell Biol ; 160: 365-380, 2020.
Article in English | MEDLINE | ID: mdl-32896328

ABSTRACT

Recent advancements in microscopy and biological technologies have allowed scientists to study dynamic plant developmental processes with high temporal and spatial resolution. Pavement cells, epidermal cells found on leaf tissue, form complex shapes with alternating regions of indentations and outgrowths that are postulated to be driven by the microtubule cytoskeleton. Given their complex shapes, pavement cells and the microtubule contribution towards morphogenesis have been of great interest in the field of developmental biology. Here, we focus on two live-cell imaging methods that allow for early and long-term imaging of the cotyledon (embryonic leaf-like tissue) and leaf epidermis with minimal invasiveness in order to study microtubules throughout pavement cell morphogenesis. The methods described in this chapter can be applied to studying other developmental processes associated with cotyledon and leaf tissue.


Subject(s)
Cell Shape , Imaging, Three-Dimensional/methods , Morphogenesis , Arabidopsis/cytology , Arabidopsis/genetics , Cotyledon/cytology , Microtubules/metabolism , Plant Leaves/cytology , Plants, Genetically Modified , Specimen Handling
2.
Nat Commun ; 11(1): 4509, 2020 09 09.
Article in English | MEDLINE | ID: mdl-32908151

ABSTRACT

Glycolysis is one of the primordial pathways of metabolism, playing a pivotal role in energy metabolism and biosynthesis. Glycolytic enzymes are known to form transient multi-enzyme assemblies. Here we examine the wider protein-protein interactions of plant glycolytic enzymes and reveal a moonlighting role for specific glycolytic enzymes in mediating the co-localization of mitochondria and chloroplasts. Knockout mutation of phosphoglycerate mutase or enolase resulted in a significantly reduced association of the two organelles. We provide evidence that phosphoglycerate mutase and enolase form a substrate-channelling metabolon which is part of a larger complex of proteins including pyruvate kinase. These results alongside a range of genetic complementation experiments are discussed in the context of our current understanding of chloroplast-mitochondrial interactions within photosynthetic eukaryotes.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/physiology , Chloroplasts/enzymology , Glycolysis/physiology , Mitochondria/enzymology , Arabidopsis/cytology , Arabidopsis Proteins/genetics , Energy Metabolism/physiology , Mutation , Phosphoglycerate Mutase/genetics , Phosphoglycerate Mutase/metabolism , Phosphopyruvate Hydratase/genetics , Phosphopyruvate Hydratase/metabolism , Photosynthesis/physiology , Plants, Genetically Modified , Protein Interaction Mapping , Protein Interaction Maps/physiology , Pyruvate Kinase/genetics , Pyruvate Kinase/metabolism
3.
Comput Biol Chem ; 78: 273-281, 2019 Feb.
Article in English | MEDLINE | ID: mdl-30597438

ABSTRACT

Developing antivirals for influenza A virus (FluA) has become more challenging due to high range of antigenic mutation and increasing numbers of drug-resistant viruses. Finding a selective inhibitor to target highly conserved region of protein-protein interactions interface, thereby increasing its efficiency against drug resistant virus could be highly beneficial. In this study, we used in silico approach to derive FluAPep1 from highly conserved region, PAN-PB1C interface and generated 121 FluAPep1 analogues. Interestingly, we found that the FluAPep1 interaction region in the PAN domain are highly conserved in many FluA subtypes. Especially, FluAPep1 targets two pandemic FluA strains, H1N1/avian/2009 and H3N2/Victoria/1975. All of these FluA subtypes PAN domain (H1N1/H3N2CAN/H3N2VIC/H7N1/H7N2) were superimposed with PAN domain from H17N10 and the calculated root mean standards deviations were less than 3 Å. FlexPepDock analysis revealed that FluAPep1 exhibited higher binding affinity (score -246.155) with the PAN domain. In addition, around 86% of non-hot spot mutated peptides (FluAPep28-122) showed enhanced binding affinity with PAN domain. ToxinPred analysis confirmed that designed peptides were non-toxic. Thus, FluAPep1 and its analogues has potential to be further developed into an antiviral treatment against FluA infection.


Subject(s)
Antiviral Agents/pharmacology , Computer Simulation , DNA-Directed RNA Polymerases/metabolism , Drug Design , Influenza, Human/drug therapy , Peptides/metabolism , Antiviral Agents/chemical synthesis , Antiviral Agents/chemistry , DNA-Directed RNA Polymerases/chemistry , Humans , Influenza A virus/drug effects , Influenza A virus/enzymology , Influenza A virus/metabolism , Influenza, Human/virology , Microbial Sensitivity Tests , Molecular Structure , Peptides/chemistry , Protein Binding/drug effects
4.
ACS Appl Mater Interfaces ; 9(31): 26582-26592, 2017 Aug 09.
Article in English | MEDLINE | ID: mdl-28719176

ABSTRACT

Transition-metal molybdates have concerned enormous curiosity as supercapacitors, photocatalysts, and electrocatalysts. These materials are the best alternatives to noble-metal-based catalysts, which are generally show a limited photocatalytic and electrocatalytic activity. In addition, the antiprotozoal drug can usually pollute the environment through improper disposable and incomplete metabolism, and it is very dangerous to humans as well as aquatic animals. Therefore, here, we have studied the electrochemical determination and photodegradation of neurotoxicity clioquinol (CQL) by nanoplate-like tin molybdate (Sn(MoO4)2, denoted as SnM), which is used as both an electro- and a photocatalyst. The as-prepared catalyst delivered a highly efficient activity toward the detection and degradation of CQL. The proposed nanoplate-like SnM was prepared through a simple wet-chemical route, and its physicochemical properties were characterized by various spectroscopic and analytical techniques. As an electrochemical sensor, the SnM electrocatalyst exhibited tremendous activity for the detection of CQL in terms of lower potential and enhanced anodic peak current. In addition, it showed high selectivity, a wide linear concentration range, a lower detection limit, and good sensitivity. From the UV-vis spectroscopy study, the SnM photocatalyst delivered an excellent photocatalytic activity toward the degradation of CQL in terms of increasing contact time and reducing CQL concentration, resulting in the increasing of the degradation efficiency about 98% within 70 min under visible light irradiation and showing an appreciable stability by observation of the reusability of the catalyst.

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