Regulation of Translation of the Head Protein of T4 Bacteriophage by Specific Binding of EF-Tu to a Leader Sequence

2003 ◽  
Vol 334 (3) ◽  
pp. 349-361 ◽  
Author(s):  
Larry Snyder ◽  
Sherry Blight ◽  
Jennifer Auchtung
Keyword(s):  
Specific Binding ◽  
Leader Sequence ◽  
Regulation Of Translation ◽  
T4 Bacteriophage ◽  
Head Protein

Correlation between structural transformation and cleavage of the major head protein of T4 bacteriophage

Cell ◽  
1976 ◽  
Vol 7 (2) ◽  
pp. 191-203 ◽  
Author(s):  
U.K. Laemmli ◽  
L.A. Amos ◽  
A. Klug
Keyword(s):  
Structural Transformation ◽  
T4 Bacteriophage ◽  
Head Protein

scholarly journals Oriented Immobilization of Bacteriophages for Biosensor Applications

2009 ◽  
Vol 76 (2) ◽  
pp. 528-535 ◽  
Author(s):  
M. Tolba ◽  
O. Minikh ◽  
L. Y. Brovko ◽  
S. Evoy ◽  
M. W. Griffiths
Keyword(s):  
Magnetic Beads ◽  
Protein Gene ◽  
Specific Binding ◽  
Burst Size ◽  
Bacteriophage T4 ◽  
Host Bacterium ◽  
Capsid Protein Gene ◽  
Phage Display Technique ◽  
Oriented Immobilization ◽  
T4 Bacteriophage

ABSTRACT A method was developed for oriented immobilization of bacteriophage T4 through introduction of specific binding ligands into the phage head using a phage display technique. Fusion of the biotin carboxyl carrier protein gene (bccp) or the cellulose binding module gene (cbm) with the small outer capsid protein gene (soc) of T4 resulted in expression of the respective ligand on the phage head. Recombinant bacteriophages were characterized in terms of infectivity. It was shown that both recombinant phages retain their lytic activity and host range. However, phage head modification resulted in a decreased burst size and an increased latent period. The efficiency of bacteriophage immobilization with streptavidin-coated magnetic beads and cellulose-based materials was investigated. It was shown that recombinant bacteriophages form specific and strong bonds with their respective solid support and are able to specifically capture and infect the host bacterium. Thus, the use of immobilized BCCP-T4 bacteriophage for an Escherichia coli B assay using a phage multiplication approach and real-time PCR allowed detection of as few as 800 cells within 2 h.

A site in the T4 bacteriophage major head protein gene that can promote the inhibition of all translation in Escherichia coli

1990 ◽  
Vol 213 (3) ◽  
pp. 477-494 ◽  
Author(s):  
Kristin J. Bergsland ◽  
Cheng Kao ◽  
Yuen-Tsu Nicco Yu ◽  
Rajiv Gulati ◽  
Larry Snyder
Keyword(s):  
Escherichia Coli ◽  
Protein Gene ◽  
T4 Bacteriophage ◽  
A Site ◽  
Head Protein

scholarly journals MicroRNAs and Long Non-Coding RNAs as Potential Candidates to Target Specific Motifs of SARS-CoV-2

2021 ◽  
Vol 7 (1) ◽  
pp. 14
Author(s):  
Lucia Natarelli ◽  
Luca Parca ◽  
Tommaso Mazza ◽  
Christian Weber ◽  
Fabio Virgili ◽  
...  
Keyword(s):  
Viral Infections ◽  
Computational Study ◽  
Specific Binding ◽  
Herd Immunity ◽  
Leader Sequence ◽  
Effective Vaccine ◽  
Viral Gene ◽  
Success Rates ◽  
Sequence Recognition ◽  
Non Coding Rnas

The respiratory system is one of the most affected targets of SARS-CoV-2. Various therapies have been utilized to counter viral-induced inflammatory complications, with diverse success rates. Pending the distribution of an effective vaccine to the whole population and the achievement of “herd immunity”, the discovery of novel specific therapies is to be considered a very important objective. Here, we report a computational study demonstrating the existence of target motifs in the SARS-CoV-2 genome suitable for specific binding with endogenous human micro and long non-coding RNAs (miRNAs and lncRNAs, respectively), which can, therefore, be considered a conceptual background for the development of miRNA-based drugs against COVID-19. The SARS-CoV-2 genome contains three motifs in the 5′UTR leader sequence recognized by selective nucleotides within the seed sequence of specific human miRNAs. The seed of 57 microRNAs contained a “GGG” motif that promoted leader sequence-recognition, primarily through offset-6mer sites able to promote microRNAs noncanonical binding to viral RNA. Similarly, lncRNA H19 binds to the 5′UTR of the viral genome and, more specifically, to the transcript of the viral gene Spike, which has a pivotal role in viral infection. Notably, some of the non-coding RNAs identified in our study as candidates for inhibiting SARS-CoV-2 gene expression have already been proposed against diverse viral infections, pulmonary arterial hypertension, and related diseases.

Specificity of polyribosomes in the synthesis of T4 bacteriophage head protein

Biochemistry ◽  
1968 ◽  
Vol 7 (5) ◽  
pp. 1739-1745 ◽  
Author(s):  
Joseph D. Padayatty ◽  
Ronald. Rolfe
Keyword(s):  
T4 Bacteriophage ◽  
Head Protein

The N Terminus of the Head Protein of T4 Bacteriophage Directs Proteins to the GroEL Chaperonin

2005 ◽  
Vol 345 (2) ◽  
pp. 375-386 ◽  
Author(s):  
Larry Snyder ◽  
Hye-Jeong Tarkowski
Keyword(s):  
N Terminus ◽  
T4 Bacteriophage ◽  
Head Protein

Reconstruction of Two-Dimensional Projections of GP 32*I

1981 ◽  
Vol 39 ◽  
pp. 38-39
Author(s):  
H.A. Cohen ◽  
W. Chiu ◽  
J. Hosoda
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Uranyl Acetate ◽  
Distilled Water ◽  
Acetate Solution ◽  
Two Dimensional ◽  
Parent Molecule ◽  
T4 Bacteriophage ◽  
Electron Imaging ◽  
Better Than

GP 32 (molecular weight 35000) is a T4 bacteriophage protein that destabilizes the DNA helix. The fragment GP32*I (77% of the total weight), which destabilizes helices better than does the parent molecule, crystallizes as platelets thin enough for electron diffraction and electron imaging. In this paper we discuss the structure of this protein as revealed in images reconstructed from stained and unstained crystals.Crystals were prepared as previously described. Crystals for electron microscopy were pelleted from the buffer suspension, washed in distilled water, and resuspended in 1% glucose. Two lambda droplets were placed on grids over freshly evaporated carbon, allowed to sit for five minutes, and then were drained. Stained crystals were prepared the same way, except that prior to draining the droplet, two lambda of aqueous 1% uranyl acetate solution were applied for 20 seconds. Micrographs were produced using less than 2 e/Å2 for unstained crystals or less than 8 e/Å2 for stained crystals.

Ultrastructural Localization of Antigens by Capillary Action Immunocytochemistry

1996 ◽  
Vol 54 ◽  
pp. 40-41
Author(s):  
László G. Kömüves
Keyword(s):  
San Francisco ◽  
Colloidal Gold ◽  
Specific Binding ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Uranyl Acetate ◽  
Adhesive Tape ◽  
Distilled Water ◽  
Capillary Action ◽  
Rabbit Igg

Light microscopic immunohistochemistry based on the principle of capillary action staining is a widely used method to localize antigens. Capillary action immunostaining, however, has not been tested or applied to detect antigens at the ultrastructural level. The aim of this work was to establish a capillary action staining method for localization of intracellular antigens, using colloidal gold probes.Post-embedding capillary action immunocytochemistry was used to detect maternal IgG in the small intestine of newborn suckling piglets. Pieces of the jejunum of newborn piglets suckled for 12 h were fixed and embedded into LR White resin. Sections on nickel grids were secured on a capillary action glass slide (100 μm wide capillary gap, Bio-Tek Solutions, Santa Barbara CA, distributed by CMS, Houston, TX) by double sided adhesive tape. Immunolabeling was performed by applying reagents over the grids using capillary action and removing reagents by blotting on filter paper. Reagents for capillary action staining were from Biomeda (Foster City, CA). The following steps were performed: 1) wet the surface of the sections with automation buffer twice, 5 min each; 2) block non-specific binding sites with tissue conditioner, 10 min; 3) apply first antibody (affinity-purified rabbit anti-porcine IgG, Sigma Chem. Co., St. Louis, MO), diluted in probe diluent, 1 hour; 4) wash with automation buffer three times, 5 min each; 5) apply gold probe (goat anti-rabbit IgG conjugated to 10 nm colloidal gold, Zymed Laboratories, South San Francisco, CA) diluted in probe diluent, 30 min; 6) wash with automation buffer three times, 5 min each; 7) post-fix with 5% glutaraldehyde in PBS for 10 min; 8) wash with PBS twice, 5 min each; 9) contrast with 1% OSO4 in PBS for 15 min; 10) wash with PBS followed by distilled water for5 min each; 11) stain with 2% uranyl acetate for 10 min; 12) stain with lead citrate for 2 min; 13) wash with distilled water three times, 1 min each. The glass slides were separated, and the grids were air-dried, then removed from the adhesive tape. The following controls were used to ensure the specificity of labeling: i) omission of the first antibody; ii) normal rabbit IgG in lieu of first antibody; iii) rabbit anti-porcine IgG absorbed with porcine IgG.

On the Role of Transferrin in 67Ga Uptake by Tumor Cells

1988 ◽  
Vol 27 (04) ◽  
pp. 151-153
Author(s):  
P. Thouvenot ◽  
F. Brunotte ◽  
J. Robert ◽  
L. J. Anghileri
Keyword(s):  
Specific Binding ◽  
Subcellular Fractionation ◽  
Animal Blood ◽  
Tumor Bearing ◽  
Cell Structures ◽  
The Difference ◽  
Sarcoma Cells ◽  
In Vitro Uptake

In vitro uptake of 67Ga-citrate and 59Fe-citrate by DS sarcoma cells in the presence of tumor-bearing animal blood plasma showed a dramatic inhibition of both 67Ga and 59Fe uptakes: about ii/io of 67Ga and 1/5o of the 59Fe are taken up by the cells. Subcellular fractionation appears to indicate no specific binding to cell structures, and the difference of binding seems to be related to the transferrin chelation and transmembrane transport differences

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