scholarly journals HvPAA1 Encodes a P-Type ATPase, a Novel Gene for Cadmium Accumulation and Tolerance in Barley (Hordeum vulgare L.)

2019 ◽  
Vol 20 (7) ◽  
pp. 1732 ◽  
Author(s):  
Xin-Ke Wang ◽  
Xue Gong ◽  
Fangbin Cao ◽  
Yizhou Wang ◽  
Guoping Zhang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization ◽  
Cadmium Accumulation ◽  
Hordeum Vulgare L ◽  
Dh Population ◽  
Cd Accumulation ◽  
Novel Gene ◽  
Cd Tolerance ◽  
P Type

The identification of gene(s) that are involved in Cd accumulation/tolerance is vital in developing crop cultivars with low Cd accumulation. We developed a doubled haploid (DH) population that was derived from a cross of Suyinmai 2 (Cd-sensitive) × Weisuobuzhi (Cd-tolerant) to conduct quantitative trait loci (QTL) mapping studies. We assessed chlorophyll content, traits that are associated with development, metal concentration, and antioxidative enzyme activity in DH population lines and parents under control and Cd stress conditions. A single QTL, designated as qShCd7H, was identified on chromosome 7H that was linked to shoot Cd concentration; qShCd7H explained 17% of the phenotypic variation. Comparative genomics, map-based cloning, and gene silencing were used in isolation, cloning, and functional characterization of the candidate gene. A novel gene HvPAA1, being related to shoot Cd concentration, was identified from qShCd7H. Sequence comparison indicated that HvPAA1 carried seven domains with an N-glycosylation motif. HvPAA1 is predominantly expressed in shoots. Subcellular localization verified that HvPAA1 is located in plasma membrane. The silencing of HvPAA1 resulted in growth inhibition, greater Cd accumulation, and a significant decrease in Cd tolerance. We conclude HvPAA1 is a novel plasma membrane-localized ATPase that contributes to Cd tolerance and accumulation in barley. The results provide us with new insights that may aid in the screening and development of Cd-tolerant and low-Cd-accumulation crops.

scholarly journals Characterization of the plasma-membrane calcium pump from Trypanosoma cruzi

1995 ◽  
Vol 306 (1) ◽  
pp. 299-303 ◽  
Author(s):  
G Benaim ◽  
S N J Moreno ◽  
G Hutchinson ◽  
V Cervino ◽  
T Hermoso ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Mammalian Cells ◽  
Membrane Vesicles ◽  
High Sensitivity ◽  
Bovine Brain ◽  
Calcium Pump ◽  
Plasma Membrane Vesicles ◽  
P Type

Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh, Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca(2+)-ATPases of different trypanosomatids differ from the Ca2+ pumps present in mammalian cells, Trypanosoma cruzi plasma-membrane Ca(2+)-ATPase shares several characteristics with the Ca2+ pumps present in other systems. This enzyme could be partially purified from epimastigote plasma-membrane vesicles using calmodulin-agarose affinity chromatography. The activity of the partially purified enzyme was stimulated by T. cruzi or bovine brain calmodulin. In addition, the enzyme cross-reacted with antiserum and monoclonal antibody 5F10 raised against human red-blood-cell Ca(2+)-ATPase, has a molecular mass of 140 kDa and forms Ca(2+)-dependent hydroxylamine-sensitive phosphorylated intermediates. These results, together with its high sensitivity to vanadate, indicate that this enzyme belongs to the P-type class of ionic pumps.

scholarly journals Functional characterization of a novel plasma membrane intrinsic protein2 in barley

2012 ◽  
Vol 7 (12) ◽  
pp. 1648-1652 ◽  
Author(s):  
Mineo Shibasaka ◽  
Sizuka Sasano ◽  
Sigeko Utsugi ◽  
Maki Katsuhara
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization

Functional characterization of a plasma membrane Na+/H+ antiporter from alkali grass (Puccinellia tenuiflora)

2010 ◽  
Vol 38 (7) ◽  
pp. 4813-4822 ◽  
Author(s):  
Xin Wang ◽  
Ru Yang ◽  
Baichen Wang ◽  
Guifeng Liu ◽  
Chuanping Yang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization ◽  
Puccinellia Tenuiflora

Identification and functional characterization of pfm, a novel gene involved in swimming motility of Pseudomonas aeruginosa

Gene ◽  
2007 ◽  
Vol 401 (1-2) ◽  
pp. 19-27 ◽  
Author(s):  
Fang Bai ◽  
Yingli Li ◽  
Haijing Xu ◽  
Huiming Xia ◽  
Tengfei Yin ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Swimming Motility ◽  
Novel Gene

scholarly journals RsSOS1 Responding to Salt Stress Might Be Involved in Regulating Salt Tolerance by Maintaining Na+ Homeostasis in Radish (Raphanus sativus L.)

Horticulturae ◽  
2021 ◽  
Vol 7 (11) ◽  
pp. 458
Author(s):  
Wanting Zhang ◽  
Jingxue Li ◽  
Junhui Dong ◽  
Yan Wang ◽  
Liang Xu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Salt Tolerance ◽  
Functional Characterization ◽  
Vital Role ◽  
Salt Stress Response ◽  
Reading Frame ◽  
Yield And Quality

Radish is a kind of moderately salt-sensitive vegetable. Salt stress seriously decreases the yield and quality of radish. The plasma membrane Na+/H+ antiporter protein Salt Overly Sensitive 1 (SOS1) plays a crucial role in protecting plant cells against salt stress, but the biological function of the RsSOS1 gene in radish remains to be elucidated. In this study, the RsSOS1 gene was isolated from radish genotype ‘NAU-TR17’, and contains an open reading frame of 3414 bp encoding 1137 amino acids. Phylogenetic analysis showed that RsSOS1 had a high homology with BnSOS1, and clustered together with Arabidopsis plasma membrane Na+/H+ antiporter (AtNHX7). The result of subcellular localization indicated that the RsSOS1 was localized in the plasma membrane. Furthermore, RsSOS1 was strongly induced in roots of radish under 150 mmol/L NaCl treatment, and its expression level in salt-tolerant genotypes was significantly higher than that in salt-sensitive ones. In addition, overexpression of RsSOS1 in Arabidopsis could significantly improve the salt tolerance of transgenic plants. Meanwhile, the transformation of RsSOS1△999 could rescue Na+ efflux function of AXT3 yeast. In summary, the plasma membrane Na+/H+ antiporter RsSOS1 plays a vital role in regulating salt-tolerance of radish by controlling Na+ homeostasis. These results provided useful information for further functional characterization of RsSOS1 and facilitate clarifying the molecular mechanism underlying salt stress response in radish.

scholarly journals Two Novel Classes of Enzymes Are Required for the Biosynthesis of Aurofusarin in Fusarium graminearum

2011 ◽  
Vol 286 (12) ◽  
pp. 10419-10428 ◽  
Author(s):  
Rasmus J. N. Frandsen ◽  
Claes Schütt ◽  
Birgitte W. Lund ◽  
Dan Staerk ◽  
John Nielsen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fusarium Graminearum ◽  
Polyketide Synthase ◽  
Functional Characterization ◽  
Extracellular Enzyme ◽  
Gene Replacement ◽  
Orphan Genes ◽  
Pigment Biosynthesis ◽  
Targeted Gene Replacement

Previous studies have reported the functional characterization of 9 out of 11 genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyze the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated γ-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF, or aurO genes in the aurofusarin cluster are deleted. Based on the shared phenotype and predicted subcellular localization, we propose that AurS is a member of an extracellular enzyme complex (GIP1-AurF-AurO-AurS) responsible for converting rubrofusarin into aurofusarin. This implies that rubrofusarin, rather than aurofusarin, is pumped across the plasma membrane. Replacement of the putative aurofusarin pump aurT increased the rubrofusarin-to- aurofusarin ratio, supporting that rubrofusarin is normally pumped across the plasma membrane. These results provide functional information on two novel classes of proteins and their contribution to polyketide pigment biosynthesis.

Functional characterization of the copper-transporting P-type ATPase gene of Penicillium janthinellum strain GXCR

2009 ◽  
Vol 47 (6) ◽  
pp. 736-745 ◽  
Author(s):  
Hongmin Lai ◽  
Changbin Sun ◽  
Huaying Tang ◽  
Xianwei Fan ◽  
Yili Ma ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Penicillium Janthinellum ◽  
Atpase Gene ◽  
P Type

Functional characterization of a wheat plasma membrane Na+/H+ antiporter in yeast

2008 ◽  
Vol 473 (1) ◽  
pp. 8-15 ◽  
Author(s):  
Haixia Xu ◽  
Xingyu Jiang ◽  
Kehui Zhan ◽  
Xiyong Cheng ◽  
Xinjian Chen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization

Functional characterization of NIPA2, a selective Mg2+ transporter

2008 ◽  
Vol 295 (4) ◽  
pp. C944-C953 ◽  
Author(s):  
Angela Goytain ◽  
Rochelle M. Hines ◽  
Gary A. Quamme
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization ◽  
Affinity Constant ◽  
Fluorescence Studies ◽  
Low Magnesium ◽  
Early Endosomes ◽  
Electrode Voltage ◽  
Voltage Dependent ◽  
Transmembrane Regions

We used microarray analysis to identify renal cell transcripts that were upregulated with low magnesium. One transcript, identified as NIPA2 (nonimprinted in Prader-Willi/Angelman syndrome) subtype 2, was increased over twofold relative to cells cultured in normal magnesium. The deduced sequence comprises 129 amino acids with 8 predicted transmembrane regions. As the secondary structure of NIPA2 conformed to a membrane transport protein, we expressed it in Xenopus oocytes and determined that it mediated Mg2+ uptake with two-electrode voltage-clamp and fluorescence studies. Mg2+ transport was electrogenic, voltage dependent, and saturable, demonstrating a Michaelis affinity constant of 0.31 mM. Unlike other reported Mg2+ transporters, NIPA2 was very selective for the Mg2+ cation. NIPA2 mRNA is found in many tissues but particularly abundant in renal cells. With the use of immunofluorescence, it was shown that NIPA2 protein was normally localized to the early endosomes and plasma membrane and was recruited to the plasma membrane in response to low extracellular magnesium. We conclude that NIPA2 plays a role in magnesium metabolism and regulation of renal magnesium conservation.

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