scholarly journals Expressing Arabidopsis thaliana V-ATPase subunit C in barley (Hordeum vulgare) improves plant performance under saline condition by enabling better osmotic adjustment

2017 ◽  
Vol 44 (12) ◽  
pp. 1147 ◽  
Author(s):  
Getnet D. Adem ◽  
Stuart J. Roy ◽  
Yuqing Huang ◽  
Zhong-Hua Chen ◽  
Feifei Wang ◽  
...  
Keyword(s):  
Grain Yield ◽  
Osmotic Adjustment ◽  
Vacuolar Atpase ◽  
Plant Performance ◽  
Organic Osmolytes ◽  
Atpase Subunit ◽  
Subunit C ◽  
Genes Encoding ◽  
Transgenic Lines ◽  
Atpase Subunits

Salinity is a global problem affecting agriculture that results in an estimated US$27 billion loss in revenue per year. Overexpression of vacuolar ATPase subunits has been shown to be beneficial in improving plant performance under saline conditions. Most studies, however, have not shown whether overexpression of genes encoding ATPase subunits results in improvements in grain yield, and have not investigated the physiological mechanisms behind the improvement in plant growth. In this study, we constitutively expressed Arabidopsis Vacuolar ATPase subunit C (AtVHA-C) in barley. Transgenic plants were assessed for agronomical and physiological characteristics, such as fresh and dry biomass, leaf pigment content, stomatal conductance, grain yield, and leaf Na+ and K+ concentration, when grown in either 0 or 300 mM NaCl. When compared with non-transformed barley, AtVHA-C expressing barley lines had a smaller reduction in both biomass and grain yield under salinity stress. The transgenic lines accumulated Na+ and K+ in leaves for osmotic adjustment. This in turn saves energy consumed in the synthesis of organic osmolytes that otherwise would be needed for osmotic adjustment.

scholarly journals RNA Interference of Genes Encoding the Vacuolar-ATPase in Liriomyza trifolii

Insects ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 41
Author(s):  
Ya-Wen Chang ◽  
Yu-Cheng Wang ◽  
Xiao-Xiang Zhang ◽  
Junaid Iqbal ◽  
Yu-Zhou Du
Keyword(s):  
Rna Interference ◽  
Expression Analysis ◽  
Target Genes ◽  
Fluorescent Protein ◽  
Control Strategies ◽  
Vacuolar Atpase ◽  
Invasive Pest ◽  
Liriomyza Trifolii ◽  
Horticultural Crops ◽  
Genes Encoding

The leafminer fly, Liriomyza trifolii, is an invasive pest of vegetable and horticultural crops in China. In this study, a microinjection method based on dsRNA was developed for RNA interference (RNAi) in L. trifolii using genes encoding vacuolar-ATPase (V-ATPase). Expression analysis indicated that V-ATPase B and V-ATPase D were more highly expressed in L. trifolii adults than in larvae or pupae. Microinjection experiments with dsV-ATPase B and dsV-ATPase D were conducted to evaluate the efficacy of RNAi in L. trifolii adults. Expression analysis indicated that microinjection with 100 ng dsV-ATPase B or dsV-ATPase led to a significant reduction in V-ATPase transcripts as compared to that of the dsGFP control (dsRNA specific to green fluorescent protein). Furthermore, lower dsRNA concentrations were also effective in reducing the expression of target genes when delivered by microinjection. Mortality was significantly higher in dsV-ATPase B- and dsV-ATPase D-treated insects than in controls injected with dsGFP. The successful deployment of RNAi in L. trifolii will facilitate functional analyses of vital genes in this economically-important pest and may ultimately result in new control strategies.

scholarly journals Identification of the ATPase Subunit of the Primary Maltose Transporter in the Hyperthermophilic Anaerobe Thermotoga maritima

2017 ◽  
Vol 83 (18) ◽  
Author(s):  
Raghuveer Singh ◽  
Derrick White ◽  
Paul Blum
Keyword(s):  
Thermotoga Maritima ◽  
Mutant Cell ◽  
Sugar Metabolism ◽  
Genetic System ◽  
Gene Replacement ◽  
Atpase Subunit ◽  
Content Type ◽  
Fermentative Hydrogen Production ◽  
Atpase Subunits ◽  
Fermentative Hydrogen

ABSTRACT Thermotoga maritima is a hyperthermophilic anaerobic bacterium that produces molecular hydrogen (H2) by fermentation. It catabolizes a broad range of carbohydrates through the action of diverse ABC transporters. However, in T. maritima and related species, highly similar genes with ambiguous annotation obscure a precise understanding of genome function. In T. maritima, three putative malK genes, all annotated as ATPase subunits, exhibited high identity to each other. To distinguish between these genes, malK disruption mutants were constructed by gene replacement, and the resulting mutant cell lines were characterized. Only a disruption of malK3 produced a defect in maltose catabolism. To verify that the mutant phenotype arose specifically from malK3 inactivation, the malK3 mutation was repaired by recombination, and maltose catabolism was restored. This study demonstrates the importance of a maltose ABC-type transporter and its relationship to sugar metabolism in T. maritima. IMPORTANCE The application and further development of a genetic system was used here to investigate gene paralogs in the hyperthermophile Thermotoga maritima. The occurrence of three ABC transporter ATPase subunits all annotated as malK was evaluated using a combination of genetic and bioinformatic approaches. The results clarify the role of only one malK gene in maltose catabolism in a nonmodel organism noted for fermentative hydrogen production.

scholarly journals Two related ARID family proteins are alternative subunits of human SWI/SNF complexes

2004 ◽  
Vol 383 (2) ◽  
pp. 319-325 ◽  
Author(s):  
Xiaomei WANG ◽  
Norman G. NAGL ◽  
Deborah WILSKER ◽  
Michael VAN SCOY ◽  
Stephen PACCHIONE ◽  
...  
Keyword(s):  
Dna Binding ◽  
Direct Evidence ◽  
Potential Interaction ◽  
Atpase Subunit ◽  
Reading Frame ◽  
Atpase Subunits ◽  
A Subunit ◽  
Distinct Subunit ◽  
Binding Behaviour

p270 (ARID1A) is a member of the ARID family of DNA-binding proteins and a subunit of human SWI/SNF-related complexes, which use the energy generated by an integral ATPase subunit to remodel chromatin. ARID1B is an independent gene product with an open reading frame that is more than 60% identical with p270. We have generated monoclonal antibodies specific for either p270 or ARID1B to facilitate the investigation of ARID1B and its potential interaction with human SWI/SNF complexes in vivo. Immunocomplex analysis provides direct evidence that endogenous ARID1B is associated with SWI/SNF-related complexes and indicates that p270 and ARID1B, similar to the ATPase subunits BRG1 and hBRM, are alternative, mutually exclusive subunits of the complexes. The ARID-containing subunits are not specific to the ATPases. Each associates with both BRG1 and hBRM, thus increasing the number of distinct subunit combinations known to be present in cells. Analysis of the panels of cell lines indicates that ARID1B, similar to p270, has a broad tissue distribution. The ratio of p270/ARID1B in typical cells is approx. 3.5:1, and BRG1 is distributed proportionally between the two ARID subunits. Analysis of DNA-binding behaviour indicates that ARID1B binds DNA in a non-sequence-specific manner similar to p270.

Streptococcus salivarius Isolates of Varying Acid Tolerance Exhibit F1F0-ATPase Conservation

2021 ◽  
pp. 1-4
Author(s):  
Lauren L. Allen ◽  
Nicholas C.K. Heng ◽  
Geoffrey R. Tompkins
Keyword(s):  
Molecular Structure ◽  
Amino Acid ◽  
Acid Tolerance ◽  
Mutans Streptococci ◽  
Streptococcus Salivarius ◽  
Synonymous Substitutions ◽  
Carious Lesions ◽  
Genes Encoding ◽  
Atpase Subunits ◽  
Membrane Bound

Genes encoding the subunits of the membrane-bound F<sub>1</sub>F<sub>0</sub>-ATPase (responsible for exporting protons from the cytoplasm and contributing to acid tolerance) were sequenced for 24 non-mutans streptococci isolated from carious lesions. Isolates, mostly <i>Streptococcus salivarius</i>, displayed a continuum of acid tolerance thresholds ranging from pH 4.55 to 3.39, but amino acid alignments of F<sub>1</sub>F<sub>0</sub>-ATPase subunits revealed few non-synonymous substitutions and these were unrelated to acid tolerance. Thus, the F<sub>1</sub>F<sub>0</sub>-ATPase is highly-conserved among <i>S. salivarius</i> isolates despite varying acid tolerance thresholds, supporting the contention that acid tolerance is determined by the level of gene/protein expression rather than variation in molecular structure.

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