scholarly journals Transmission Electron Microscopy Identification of VPH16 L1 His-Tag Inclusion Bodies in Escherichia Coli SHuffle T7

2020 ◽  
Vol 26 (S1) ◽  
pp. 193-194
Author(s):  
Sandra Rodríguez ◽  
Odelsa Ancheta ◽  
Yunier Serrano ◽  
Adriana Otero ◽  
Viviana Falcón ◽  
...  
2005 ◽  
Vol 187 (10) ◽  
pp. 3599-3601 ◽  
Author(s):  
M. Mar Carrió ◽  
Antonio Villaverde

ABSTRACT By immunostaining and transmission electron microscopy, chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively. Functional implications of this distinct localization are discussed in the context of Escherichia coli protein quality control.


2013 ◽  
Vol 76 (4) ◽  
pp. 560-567 ◽  
Author(s):  
Y. WANG ◽  
L. JIN ◽  
K. H. OMINSKI ◽  
M. HE ◽  
Z. XU ◽  
...  

Tannins from forages grown (n = 10) on the Canadian prairie, as well as from Quebracho, Rhus semialata, and brown seaweed (Ascophyllum nodosum), were screened for anti–Escherichia coli O157:H7 activity against E. coli O157:H7 strain 3081 at a concentration of 400 μg/ml for each tannin type, except for brown seaweed, which was at 50 μg/ml. Growth of the bacteria was assessed by measuring the optical density at 600 nm over 24 h. Tannin from seaweed at a concentration of 50 μg/ml inhibited growth of strain 3081. Among the terrestrial forages, only condensed tannins (CT) from purple prairie clover (Dalea purpurea Vent; PPC) increased (P < 0.05) the lag time and reduced (P < 0.05) the growth rate of E. coli O157:H7. The anti–E. coli O157:H7 activity of PPC CT was further assessed by culturing E. coli strain ATCC 25922 and eight strains of E. coli O157:H7 with PPC CT at 0, 25, 50, 100, or 200 μg/ml. Selected strains were enumerated after 0, 6, and 24 h of incubation, and fatty acid composition was determined after 24 h of incubation. E. coli strain 25922 was cultured with 0, 50, or 200 μg of CT per ml and harvested during the exponential growth phase for examination by transmission electron microscopy. Increasing CT concentration linearly increased (P < 0.001) the lag times of seven strains and linearly reduced (P < 0.001) the growth rates of eight E. coli O157:H7 strains. Proportions of unsaturated fatty acids in the total fatty acids were decreased (P < 0.01) by CT at 50 μg/ml. Transmission electron microscopy showed that CT disrupted the outer membrane structure. Anti–E. coli O157:H7 activity of PPC CT at levels of up to 200 μg/ml was bacteriostatic rather than bactericidal, and the mechanism of anti–E. coli activity may involve alteration in the fatty acid composition and disruption of the outer membrane of the cell.


Parasitology ◽  
1984 ◽  
Vol 89 (1) ◽  
pp. 71-78 ◽  
Author(s):  
B. Leitch ◽  
A. J. Probert ◽  
N. W. Runham

SummaryThe ultrastructure of the tegument of Schistosoma haematobium was examined using scanning and transmission electron microscopy. The surface of the male worm is characterized by numerous raised tubercles bearing apically directed spines. The female in contrast to the male is cylindrical and relatively smooth. Details of oral and ventral suckers are given. The use of uranyl acetate as a tertiary fixative and en bloc stain has revealed the heptalaminate nature of the outer membrane. Tegumental mitochondria are shown to be morphologically more complex than those of S. mansoni. Spherical and elliptical inclusion bodies are also described. The ultrastructure of the oesophageal tegument of S. haematobium is described for the first time and corresponds with earlier observations of S. mansoni.


2006 ◽  
Vol 17 (12) ◽  
pp. 5063-5074 ◽  
Author(s):  
Iain L. Mainprize ◽  
Daniel R. Beniac ◽  
Elena Falkovskaia ◽  
Robert M. Cleverley ◽  
Lila M. Gierasch ◽  
...  

Structural studies on various domains of the ribonucleoprotein signal recognition particle (SRP) have not converged on a single complete structure of bacterial SRP consistent with the biochemistry of the particle. We obtained a three-dimensional structure for Escherichia coli SRP by cryoscanning transmission electron microscopy and mapped the internal RNA by electron spectroscopic imaging. Crystallographic data were fit into the SRP reconstruction, and although the resulting model differed from previous models, they could be rationalized by movement through an interdomain linker of Ffh, the protein component of SRP. Fluorescence resonance energy transfer experiments determined interdomain distances that were consistent with our model of SRP. Docking our model onto the bacterial ribosome suggests a mechanism for signal recognition involving interdomain movement of Ffh into and out of the nascent chain exit site and suggests how SRP could interact and/or compete with the ribosome-bound chaperone, trigger factor, for a nascent chain during translation.


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