A 13-kilodalton maize mitochondrial protein in E. coli confers sensitivity to Bipolaris maydis toxin

Science ◽  
1988 ◽  
Vol 239 (4837) ◽  
pp. 293-295 ◽  
Author(s):  
R. Dewey ◽  
J. Siedow ◽  
D. Timothy ◽  
C. Levings
Keyword(s):  
Mitochondrial Protein ◽  
Bipolaris Maydis ◽  
E Coli

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1988 ◽  
Vol 8 (1) ◽  
pp. 371-380
Author(s):  
T W McMullin ◽  
R L Hallberg
Keyword(s):  
Escherichia Coli ◽  
Tetrahymena Thermophila ◽  
Mitochondrial Protein ◽  
Cross Reactivity ◽  
Macromolecular Complexes ◽  
E Coli ◽  
Groel Gene ◽  
Evolutionarily Conserved ◽  
Associated Proteins ◽  
Related Proteins

We recently reported that a Tetrahymena thermophila 58-kilodalton (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Escherichia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.

scholarly journals A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.

1988 ◽  
Vol 8 (1) ◽  
pp. 371-380 ◽  
Author(s):  
T W McMullin ◽  
R L Hallberg
Keyword(s):  
Escherichia Coli ◽  
Tetrahymena Thermophila ◽  
Mitochondrial Protein ◽  
Cross Reactivity ◽  
Macromolecular Complexes ◽  
E Coli ◽  
Groel Gene ◽  
Evolutionarily Conserved ◽  
Associated Proteins ◽  
Related Proteins

We recently reported that a Tetrahymena thermophila 58-kilodalton (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Escherichia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.

Inhibition of mitochondrial and bacterial protein synthesis by chloramphenicol

1970 ◽  
Vol 48 (4) ◽  
pp. 479-485 ◽  
Author(s):  
K. B. Freeman
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Bacterial Protein ◽  
E Coli ◽  
Inhibition Of Protein Synthesis ◽  
Acetyl Group ◽  
Bacterial Protein Synthesis ◽  
Escherichia Coli B

The structural requirements for the inhibition of protein synthesis in mitochondria and in bacterial extracts by chloramphenicol isomers and analogues are similar. D-threo-Chloramphenicol and its p-methylthio, p-methylsulfonyl, and p-sulfamoyl analogues equally inhibit protein synthesis in isolated rat-liver mitochondria and extracts of Escherichia coli B. Fifty percent inhibition is at 15 μM and 10 μM, respectively. Analogues with larger p-substituents on the phenyl ring or with an m-chloro group are less inhibitory in both systems. L-threo-Chloramphenicol and deacylated chloramphenicol do not inhibit mitochondrial protein synthesis; with a dichloroacetyl group replacing the acetyl group on chloramphenicol 50% inhibition is at 65 μM, and L-erythro-chloramphenicol is 2% as inhibitory as D-threo-chloramphenicol. The inhibition of protein synthesis in intact E. coli B is in the order: chloramphenicol > p-methylthio > p-methylsulfonyl > p-sulfamoyl, 50% inhibition being at 4 μM for chloramphenicol.

Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (PUMP) expressed in E. coli

2000 ◽  
Vol 28 (5) ◽  
pp. A187-A187
Author(s):  
Jiri Borecky ◽  
Ivan G. Maia ◽  
Alexandre D. T. Costa ◽  
Paula Bresciani Martins de Andrade ◽  
Petr Jezek ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Mitochondrial Protein ◽  
E Coli ◽  
Plant Uncoupling Mitochondrial Protein

scholarly journals The ATP synthase subunit β (ATP5B) is an entry factor for the hepatitis E virus

2016 ◽  
Author(s):  
Zulfazal Ahmed ◽  
Prasida Holla ◽  
Imran Ahmad ◽  
Shahid Jameel
Keyword(s):  
Atp Synthase ◽  
Hepatitis E Virus ◽  
Viral Infections ◽  
Rna Virus ◽  
High Titer ◽  
Mitochondrial Protein ◽  
Hepatitis E ◽  
E Coli ◽  
Mass Spectrometric Approach

AbstractHepatitis E occurs sporadically and as outbreaks due to contamination of drinking water. The causative agent, hepatitis E virus (HEV) is a hepatotropic non-enveloped RNA virus, which grows poorlyin vitro.Consequently, many aspects of HEV biology are poorly characterized, including its cellular receptor and entry mechanism(s). Previous studies from our laboratory have shown that heparan sulfate proteoglycans (HSPGs) act as attachment factors for the virus. In the absence of purified high titer infectious virus, we have used hepatitis E virus-like particles (HEV-LPs) expressed and purified fromE. colito identify HEV entry factor(s) on liver cells in culture. Using a pull down and mass spectrometric approach, we identified the ATP synthase subunit β (ATP5B) to bind the HEV capsid protein. Its role in the entry of HEV was then validated using antibody and siRNA mediated approaches, and infectious HEV from the stools of a hepatitis E patient. Though ATP synthase is largely a mitochondrial protein, the cell surface expressed form of ATP5B is implicated in other viral infections.

scholarly journals Frataxins Emerge as New Players of the Intracellular Antioxidant Machinery

Antioxidants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 315
Author(s):  
Ana Belén Uceda ◽  
Josefa Donoso ◽  
Juan Frau ◽  
Bartolomé Vilanova ◽  
Miquel Adrover
Keyword(s):  
Oxidative Stress ◽  
Iron Homeostasis ◽  
Mitochondrial Protein ◽  
Oxygen Species ◽  
E Coli ◽  
Intracellular Proteins ◽  
Direct Binding ◽  
Endogenous Antioxidants ◽  
And Oxidative Stress ◽  
Antioxidant Machinery

Frataxin is a mitochondrial protein which deficiency causes Friedreich’s ataxia, a cardio-neurodegenerative disease. The lack of frataxin induces the dysregulation of mitochondrial iron homeostasis and oxidative stress, which finally causes the neuronal death. The mechanism through which frataxin regulates the oxidative stress balance is rather complex and poorly understood. While the absence of human (Hfra) and yeast (Yfh1) frataxins turn out cells sensitive to oxidative stress, this does not occur when the frataxin gene is knocked-out in E. coli. To better understand the biological roles of Hfra and Yfh1 as endogenous antioxidants, we have studied their ability to inhibit the formation of reactive oxygen species (ROS) from Cu2+- and Fe3+-catalyzed degradation of ascorbic acid. Both proteins drastically reduce the formation of ROS, and during this process they are not oxidized. In addition, we have also demonstrated that merely the presence of Yfh1 or Hfra is enough to protect a highly oxidation-prone protein such as α-synuclein. This unspecific intervention (without a direct binding) suggests that frataxins could act as a shield to prevent the oxidation of a broad set of intracellular proteins, and reinforces that idea that frataxin can be used to prevent neurological pathologies linked to an enhanced oxidative stress.

Endotoxin Alteration of the Mucopolysaccharide Blood Vessel Coating in Rats

1974 ◽  
Vol 32 ◽  
pp. 148-149
Author(s):  
D. E. Philpott ◽  
A. Takahashi
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Salivary Gland ◽  
Carotid Artery ◽  
Basement Membrane ◽  
Coronary Vessels ◽  
Ruthenium Red ◽  
E Coli ◽  
Old Rats ◽  
The Brain

Two month, eight month and two year old rats were treated with 10 or 20 mg/kg of E. Coli endotoxin I. P. The eight month old rats proved most resistant to the endotoxin. During fixation the aorta, carotid artery, basil arartery of the brain, coronary vessels of the heart, inner surfaces of the heart chambers, heart and skeletal muscle, lung, liver, kidney, spleen, brain, retina, trachae, intestine, salivary gland, adrenal gland and gingiva were treated with ruthenium red or alcian blue to preserve the mucopolysaccharide (MPS) coating. Five, 8 and 24 hrs of endotoxin treatment produced increasingly marked capillary damage, disappearance of the MPS coating, edema, destruction of endothelial cells and damage to the basement membrane in the liver, kidney and lung.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

Emigration of neutrophils in the central nervous system

1983 ◽  
Vol 41 ◽  
pp. 788-789
Author(s):  
John L.Beggs ◽  
John D. Waggener ◽  
Wanda Miller ◽  
Jane Watkins
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Osmium Tetroxide ◽  
White Blood Cells ◽  
Arterial Perfusion ◽  
E Coli ◽  
Intracisternal Injection ◽  
The Central Nervous System ◽  
Brain And Spinal Cord ◽  
Interendothelial Junctions

Studies using mesenteric and ear chamber preparations have shown that interendothelial junctions provide the route for neutrophil emigration during inflammation. The term emigration refers to the passage of white blood cells across the endothelium from the vascular lumen. Although the precise pathway of transendo- thelial emigration in the central nervous system (CNS) has not been resolved, the presence of different physiological and morphological (tight junctions) properties of CNS endothelium may dictate alternate emigration pathways.To study neutrophil emigration in the CNS, we induced meningitis in guinea pigs by intracisternal injection of E. coli bacteria.In this model, leptomeningeal inflammation is well developed by 3 hr. After 3 1/2 hr, animals were sacrificed by arterial perfusion with 3% phosphate buffered glutaraldehyde. Tissues from brain and spinal cord were post-fixed in 1% osmium tetroxide, dehydrated in alcohols and propylene oxide, and embedded in Epon. Thin serial sections were cut with diamond knives and examined in a Philips 300 electron microscope.

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