A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. I. fitting the RNA to a 3D electron microscopic map at 20 Å 1 1Edited by D. E. Drapper

1997 ◽  
Vol 271 (4) ◽  
pp. 524-544 ◽  
Author(s):  
Florian Mueller ◽  
Richard Brimacombe
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Three Dimensional ◽  
Electron Microscopic ◽  
New Model ◽  
3D Electron ◽  
Rna I

Three-dimensional arrangement of the Escherichia coli 16 S ribosomal RNA

1985 ◽  
Vol 184 (1) ◽  
pp. 53-66 ◽  
Author(s):  
Alain Expert-Bezançon ◽  
Paul L. Wollenzien
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Three Dimensional

scholarly journals Three-Dimensional Electron Microscopic Imaging of Membrane Invaginations in Escherichia coli Overproducing the Chemotaxis Receptor Tsr

2004 ◽  
Vol 186 (15) ◽  
pp. 5052-5061 ◽  
Author(s):  
Jonathan Lefman ◽  
Peijun Zhang ◽  
Teruhisa Hirai ◽  
Robert M. Weis ◽  
Jemma Juliani ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Bacterial Chemotaxis ◽  
Molecular Architecture ◽  
Electron Microscopic ◽  
E Coli ◽  
Macromolecular Assemblies ◽  
Membrane Networks ◽  
Receptor Clusters

ABSTRACT Electron tomography is a powerful method for determining the three-dimensional structures of large macromolecular assemblies, such as cells, organelles, and multiprotein complexes, when crystallographic averaging methods are not applicable. Here we used electron tomographic imaging to determine the molecular architecture of Escherichia coli cells engineered to overproduce the bacterial chemotaxis receptor Tsr. Tomograms constructed from fixed, cryosectioned cells revealed that overproduction of Tsr led to formation of an extended internal membrane network composed of stacks and extended tubular structures. We present an interpretation of the tomogram in terms of the packing arrangement of Tsr using constraints derived from previous X-ray and electron-crystallographic studies of receptor clusters. Our results imply that the interaction between the cytoplasmic ends of Tsr is likely to stabilize the presence of the membrane networks in cells overproducing Tsr. We propose that membrane invaginations that are potentially capable of supporting axial interactions between receptor clusters in apposing membranes could also be present in wild-type E. coli and that such receptor aggregates could play an important role in signal transduction during bacterial chemotaxis.

scholarly journals Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: the distribution of ribosomal RNA.

1991 ◽  
Vol 115 (3) ◽  
pp. 597-605 ◽  
Author(s):  
J Frank ◽  
P Penczek ◽  
R Grassucci ◽  
S Srivastava
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Mass Density ◽  
Three Dimensional ◽  
Particle Method ◽  
Small Subunit ◽  
Cryo Electron Microscopy ◽  
Dimensional Reconstruction ◽  
The Masses ◽  
Complex Distribution

A reconstruction, at 40 A, of the Escherichia coli ribosome imaged by cryo-electron microscopy, obtained from 303 projections by a single-particle method of reconstruction, shows the two subunits with unprecedented clarity. In the interior of the subunits, a complex distribution of higher mass density is recognized, which is attributed to ribosomal RNA. The masses corresponding to the 16S and 23S components are linked in the region of the platform of the small subunit. Thus the topography of the rRNA regions responsible for protein synthesis can be described.

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