scholarly journals Heterologous expression of fused genes encoding the glycoprotein 5 from PRRSV: A way for producing functional protein in prokaryotic microorganism

2010 ◽  
Vol 147 (2) ◽  
pp. 130-135 ◽  
Author(s):  
Xiaofeng Ren ◽  
Mingcui Wang ◽  
Jiechao Yin ◽  
Yudong Ren ◽  
Guangxing Li
Keyword(s):  
Heterologous Expression ◽  
Functional Protein ◽  
Genes Encoding ◽  
Glycoprotein 5

scholarly journals MMP20 Hemopexin Domain Mutation in Amelogenesis Imperfecta

2009 ◽  
Vol 89 (1) ◽  
pp. 46-50 ◽  
Author(s):  
S.-K. Lee ◽  
F. Seymen ◽  
H.-Y. Kang ◽  
K.-E. Lee ◽  
K. Gencay ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Proteolytic Enzymes ◽  
Dental Enamel ◽  
Amelogenesis Imperfecta ◽  
Single Amino Acid ◽  
Functional Protein ◽  
Genes Encoding ◽  
Kallikrein 4 ◽  
Normal Thickness ◽  
Hemopexin Domain

Proteolytic enzymes serve important functions during dental enamel formation, and mutations in the kallikrein 4 ( KLK4) and enamelysin ( MMP20) genes cause autosomal-recessive amelogenesis imperfecta (ARAI). So far, only 1 KLK4 and 3 MMP20 mutations have been reported in ARAI kindreds. To determine whether ARAI in a family with a hypomaturation-type enamel defect is caused by mutations in the genes encoding enamel proteolytic enzymes, we performed mutational analysis on candidate genes. Mutational and haplotype analyses revealed an ARAI-causing point mutation (c.910G>A, p.A304T) in exon 6 of MMP20 that results in a single amino acid substitution in the hemopexin domain. Western blot analysis showed decreased expression of the mutant protein, but zymogram analysis demonstrated that this mutant was a functional protein. The proband and an affected brother were homozygous for the mutation, and both unaffected parents were carriers. The enamel of newly erupted teeth had normal thickness, but was chalky white and became darker with age.

scholarly journals Improved Squalene Production via Modulation of the Methylerythritol 4-Phosphate Pathway and Heterologous Expression of Genes from Streptomyces peucetius ATCC 27952 in Escherichia coli

2009 ◽  
Vol 75 (22) ◽  
pp. 7291-7293 ◽  
Author(s):  
Gopal Prasad Ghimire ◽  
Hei Chan Lee ◽  
Jae Kyung Sohng
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Streptomyces Peucetius ◽  
E Coli ◽  
Expression Of Genes ◽  
Genes Encoding

ABSTRACT Putative hopanoid genes from Streptomyces peucetius were introduced into Escherichia coli to improve the production of squalene, an industrially important compound. High expression of hopA and hopB (encoding squalene/phytoene synthases) together with hopD (encoding farnesyl diphosphate synthase) yielded 4.1 mg/liter of squalene. This level was elevated to 11.8 mg/liter when there was also increased expression of dxs and idi, E. coli genes encoding 1-deoxy-d-xylulose 5-phosphate synthase and isopentenyl diphosphate isomerase.

Role of the Vps9-domain protein RgfA inDictyosteliumchemotaxis and development

2013 ◽  
Vol 59 (1) ◽  
pp. 22-27
Author(s):  
Jeffrey A. Hadwiger
Keyword(s):  
Cell Growth ◽  
Heterologous Expression ◽  
Rab Proteins ◽  
Nucleotide Exchange ◽  
Surface Receptors ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factors ◽  
Genes Encoding ◽  
Redundant Functions ◽  
External Signals

Proteins with a Vps9 domain function as guanine nucleotide exchange factors for Rab proteins and can mediate the uptake of cell surface receptors or other molecules through endocytosis. However, genes encoding these proteins have not been previously studied in cells with robust chemotactic capabilities. Several genes encoding Vps9 domains were identified in the genome of Dictyostelium discoideum, and one of the genes, designated as rgfA (DDB_G0272038), was examined for functions in cell growth, development, and chemotaxis. The rgfA gene was expressed during vegetative growth and throughout development, but disruption of this gene resulted in no major alterations in cell growth, macropinocytosis, developmental morphology, or chemotactic movement. However, heterologous expression of RgfA resulted in a delay of developmental morphogenesis and impaired chemotaxis of cells to folate but did not affect macropinocytosis. These results suggest that RgfA might share redundant functions with other Dictyostelium Vps9-domain proteins and that heterologous expression of this protein can alter processes that depend on the reception of external signals.

scholarly journals Exploring the Oxygenase Function of Form II Rubisco for Production of Glycolate from CO2

2021 ◽  
Author(s):  
Fan Yang ◽  
Junli Zhang ◽  
Zhen Cai ◽  
Jie Zhou ◽  
Yin Li
Keyword(s):  
Energy Loss ◽  
Heterologous Expression ◽  
Higher Plants ◽  
Fold Increase ◽  
Riftia Pachyptila ◽  
Bisphosphate Carboxylase ◽  
Oxygenase Activity ◽  
Photosynthetic Production ◽  
Genes Encoding ◽  
Glycolate Dehydrogenase

Abstract The oxygenase activity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) converts ribulose-1,5-bisphosphate (RuBP) into 2-phosphoglycolate, which in turn channels into photorespiration, resulting in carbon and energy loss in higher plants. We observed that glycolate can be accumulated extracellularly when two genes encoding the glycolate dehydrogenase of cyanobacteria Synechocystis sp. PCC 6803 were inactivated. This inspired us to explore the oxygenase function of Rubisco for production of glycolate, an important industrial chemical, from CO2 by engineered cyanobacteria. Since the oxygenase activity of Rubisco is generally low in CO2-rich carboxysome of cyanobacteria, we introduced Form II Rubisco, which cannot be assembled in carboxysome, into the cytoplasm of cyanobacteria. Heterologous expression of a Form II Rubisco from endosymbiont of tubeworm Riftia pachyptila (RPE Rubisco) significantly increased glycolate production. We show that the RPE Rubisco is expressed in the cytoplasm. Glycolate production increased upon addition of NaHCO3 but decreased upon supplying CO2. The titer of glycolate reached 2.8 g/L in 18 days, a 14-fold increase compared with the initial strain with glycolate dehydrogenase inactivated. This is also the highest glycolate titer biotechnologically produced from CO2 ever reported. Photosynthetic production of glycolate demonstrated the oxygenase activity of Form II Rubisco can be explored for production of chemicals from CO2.

scholarly journals Heterologous Expression of Genes Encoding Bacterial Light-harvesting Complexes inRhodobacter sphaeroides

1995 ◽  
Vol 270 (40) ◽  
pp. 23875-23882 ◽  
Author(s):  
Gregory J. S. Fowler ◽  
Alastair T. Gardiner ◽  
R. Christopher Mackenzie ◽  
Stuart J. Barratt ◽  
Adrian E. Simmons ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Light Harvesting ◽  
Light Harvesting Complexes ◽  
Expression Of Genes ◽  
Genes Encoding

scholarly journals Gene-Wide Analysis of Aquaporin Gene Family in Malus domestica and Heterologous Expression of the Gene MpPIP2;1 Confers Drought and Salinity Tolerance in Arabidposis thaliana

2019 ◽  
Vol 20 (15) ◽  
pp. 3710
Author(s):  
Haili Liu ◽  
Leilei Yang ◽  
Miaomiao Xin ◽  
Fengwang Ma ◽  
Jingying Liu
Keyword(s):  
Arabidopsis Thaliana ◽  
Phylogenetic Analysis ◽  
Heterologous Expression ◽  
Small Molecules ◽  
Salinity Tolerance ◽  
Malus Domestica ◽  
Populus Trichocarpa ◽  
Integral Membrane Proteins ◽  
Aquaporin Gene ◽  
Genes Encoding

The aquaporins (AQPs) are a family of integral membrane proteins involved in the transcellular membrane transport of water and other small molecules. A scan of the apple (Malus domestica) genome revealed the presence of 42 genes encoding putative AQPs. Based on a phylogenetic analysis of the deduced peptide sequences of the AQPs generated by Arabidopsis thaliana, poplar (Populus trichocarpa), and rubber (Hevea brasiliensis), the apple AQPs were each assigned membership of the five established AQP subfamilies, namely the PIPs (eleven members), the TIPs (thirteen members), the NIPs (eleven members), the SIPs (five members), and the XIPs (two members). The apple AQPs included asparagine-proline-alanine (NPA) motifs, an aromatic/arginine (ar/R) selectivity filter, and the Froger’s positions. The heterologous expression of MpPIP2;1 in A. thaliana was shown to enhance the level of tolerance exhibited against both drought and salinity.

scholarly journals Heterologous Expression of Aedes aegypti Cation Chloride Cotransporter 2 (aeCCC2) in Xenopus laevis Oocytes Induces an Enigmatic Na+/Li+ Conductance

Insects ◽  
2019 ◽  
Vol 10 (3) ◽  
pp. 71 ◽  
Author(s):  
Megha Kalsi ◽  
Christopher Gillen ◽  
Peter Piermarini
Keyword(s):  
Plasma Membrane ◽  
Aedes Aegypti ◽  
Heterologous Expression ◽  
Xenopus Oocytes ◽  
Xenopus Laevis Oocytes ◽  
Conductive Pathway ◽  
Electrode Voltage ◽  
Genes Encoding ◽  
Voltage Clamping ◽  
Cation Chloride Cotransporters

The yellow fever mosquito Aedes aegypti possesses three genes encoding putative Na+-coupled cation chloride cotransporters (CCCs): aeNKCC1, aeCCC2, and aeCCC3. To date, none of the aeCCCs have been functionally characterized. Here we expressed aeCCC2 heterologously in Xenopus oocytes and measured the uptake of Li+ (a tracer for Na+) and Rb+ (a tracer for K+). Compared to control (H2O-injected) oocytes, the aeCCC2-expressing oocytes exhibited significantly greater uptake of Li+, but not Rb+. However, the uptake of Li+ was neither Cl−-dependent nor inhibited by thiazide, loop diuretics, or amiloride, suggesting unconventional CCC activity. To determine if the Li+-uptake was mediated by a conductive pathway, we performed two-electrode voltage clamping (TEVC) on the oocytes. The aeCCC2 oocytes were characterized by an enhanced conductance for Li+ and Na+, but not K+, compared to control oocytes. It remains to be determined whether aeCCC2 directly mediates the Na+/Li+ conductance or whether heterologous expression of aeCCC2 stimulates an endogenous cation channel in the oocyte plasma membrane.

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