Methyl 4-mercaptobutyrimidate as a cleavable crosslinking reagent and its application to the Escherichia coli 30S ribosome

Biochemistry ◽  
1973 ◽  
Vol 12 (17) ◽  
pp. 3266-3273 ◽  
Author(s):  
Robert R. Traut ◽  
Alex Bollen ◽  
Tung-Tien Sun ◽  
John W. B. Hershey ◽  
John Sundberg ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crosslinking Reagent

scholarly journals The Use of a Cleavable Crosslinking Reagent to Identify Neighboring Proteins in the 30-S Ribosomal Subunit of Escherichia coli

1976 ◽  
Vol 63 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Hava PERETZ ◽  
Harry TOWBIN ◽  
David ELSON
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Subunit ◽  
Crosslinking Reagent

IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: Identification of 30 S proteins crosslinked to IF-3—Utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide

1981 ◽  
Vol 208 (2) ◽  
pp. 554-562 ◽  
Author(s):  
Barry S. Cooperman ◽  
Alain Expert-Bezançon ◽  
Lawrence Kahan ◽  
Jacques Dondon ◽  
Marianne Grunberg-Manago
Keyword(s):  
Escherichia Coli ◽  
Two Stage ◽  
Crosslinking Reagent ◽  
S Proteins

scholarly journals Identification of a 16-S RNA Fragment Crosslinked to Protein S1 within Escherichia coli Ribosomal 30-S Subunits by the Use of a Crosslinking Reagent: Ethyl 4-Azidobenzoylaminoacetimidate

2005 ◽  
Vol 115 (3) ◽  
pp. 479-484 ◽  
Author(s):  
Barbara GOLINSKA ◽  
Régine MILLON ◽  
Claude BACKENDORF ◽  
Jean-Pierre EBEL ◽  
Bernard EHRESMANN ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crosslinking Reagent

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

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.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

The Nature of the Intramembrane Particle

1980 ◽  
Vol 38 ◽  
pp. 688-691
Author(s):  
A.J. Verkleij
Keyword(s):  
Escherichia Coli ◽  
Tight Junction ◽  
Gap Junction ◽  
The Other ◽  
Fracture Face ◽  
Band 3 Protein ◽  
Satisfactory Explanation ◽  
Freeze Fracturing ◽  
Intramembrane Particle ◽  
Luminal Membrane

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.

Cloning and high level expression of Cynodon dactylon (Bermuda grass) pollen profilin (Cyn d 12) in Escherichia coli: purification and characterization of the allergen

1997 ◽  
Vol 27 (11) ◽  
pp. 1307-1313 ◽  
Author(s):  
J. A. ASTURIAS ◽  
M. C. ARILLA ◽  
N. GOMEZ-BAYON ◽  
J. MARTINEZ ◽  
A. MARTINEZ ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Grass Pollen ◽  
Cynodon Dactylon ◽  
Bermuda Grass ◽  
Purification And Characterization ◽  
High Level Expression ◽  
Bermuda Grass Pollen ◽  
D 12 ◽  
High Level
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