Structural changes in 16S RNA from Escherichia coli upon unfolding by urea

Biopolymers ◽  
1993 ◽  
Vol 33 (11) ◽  
pp. 1747-1755 ◽  
Author(s):  
A. A. Timchenko ◽  
J. Langowski ◽  
I. N. Serdyuk
Keyword(s):  
Escherichia Coli ◽  
Structural Changes ◽  
16S Rna

Protein-induced conformational changes in 16S rRNA during assembly of the Escherichia Coli 30S ribosomal subunit: A STEM study

1987 ◽  
Vol 45 ◽  
pp. 910-911
Author(s):  
M. Boublik ◽  
V. Mandiyan ◽  
J.F. Hainfeld ◽  
J.S. Wall
Keyword(s):  
16S Rrna ◽  
Conformational Changes ◽  
Ribosomal Proteins ◽  
Structural Changes ◽  
Ribosomal Subunit ◽  
Compact Structure ◽  
E Coli ◽  
Freeze Dried ◽  
16S Rna ◽  
30S Subunit

The aim of this study is to understand the mechanism of 16S rRNA folding into the compact structure of the small 30S subunit of E. coli ribosome. The assembly of the 30S E. coli ribosomal subunit is a sequence of specific interactions of 16S rRNA with 21 ribosomal proteins (S1-S21). Using dedicated high resolution STEM we have monitored structural changes induced in 16S rRNA by the proteins S4, S8, S15 and S20 which are involved in the initial steps of 30S subunit assembly. S4 is the first protein to bind directly and stoichiometrically to 16S rRNA. Direct binding also occurs individually between 16S RNA and S8 and S15. However, binding of S20 requires the presence of S4 and S8. The RNA-protein complexes are prepared by the standard reconstitution procedure, dialyzed against 60 mM KCl, 2 mM Mg(OAc)2, 10 mM-Hepes-KOH pH 7.5 (Buffer A), freeze-dried and observed unstained in dark field at -160°.

Probing the phosphates of the Escherichia coli ribosomal 16S RNA in its naked form, in the 30S subunit, and in the 70S ribosome

Biochemistry ◽  
1989 ◽  
Vol 28 (14) ◽  
pp. 5847-5855 ◽  
Author(s):  
Florence Baudin ◽  
Marylene Mougel ◽  
Pascale Romby ◽  
Flore Eyermann ◽  
Jean Pierre Ebel ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
16S Rna ◽  
30S Subunit ◽  
70S Ribosome

THE TERMINAL GROUPS OF RIBONUCLEATE CHAINS IN EACH OF THE 16S AND 23S COMPONENTS OF ESCHERICHIA COLI RIBOSOMAL RNA

1967 ◽  
Vol 45 (6) ◽  
pp. 937-948 ◽  
Author(s):  
J. L. Nichols ◽  
B. G. Lane
Keyword(s):  
Escherichia Coli ◽  
Chain Length ◽  
Ribosomal Rna ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation ◽  
Quantitative Estimates ◽  
16S Rna ◽  
The Mean ◽  
End Group

Ribosomal ribonucleates from Escherichia coli have been resolved into 16S and 28S components by sucrose density-gradient centrifugation, and the chain termini in each of the 16S and 23S RNA components have been analyzed by hydrolysis with alkali. The principal 5′-linked end group of 16S RNA was found to be adenosine, and the principal 5′-linked end group of 23S RNA was found to be uridine. The principal 3′-linked end group of 16S RNA was also found to be adenosine, whereas the principal 3′-linked end group of 23S RNA was found to be guanosine. Quantitative estimates of chain length based on analyses for 5′-iinked terminals indicate that the mean chain length for 16S RNA is about 1.3 × 103nucleotide residues and the mean chain length for 23S RNA is about 2.1 × 103nucleotide residues.

Conversion of Escherichia coli 17S chloramphenicol RNA to a 16S RNA in vitro

Biochimie ◽  
1976 ◽  
Vol 58 (8) ◽  
pp. 1007-1009 ◽  
Author(s):  
Jacques Alain Tréton ◽  
Françoise Hayes
Keyword(s):  
Escherichia Coli ◽  
16S Rna

Ligand-dependent structural changes and limited proteolysis of Escherichia coli phosphofructokinase-2

2002 ◽  
Vol 406 (2) ◽  
pp. 289-295 ◽  
Author(s):  
Ricardo Cabrera ◽  
Victoria Guixé ◽  
Jennifer Alfaro ◽  
Patricio H Rodrı́guez ◽  
Jorge Babul
Keyword(s):  
Escherichia Coli ◽  
Structural Changes ◽  
Limited Proteolysis

scholarly journals A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes

2019 ◽  
Vol 116 (51) ◽  
pp. 25591-25601 ◽  
Author(s):  
Seungwoo Chang ◽  
Karel Naiman ◽  
Elizabeth S. Thrall ◽  
James E. Kath ◽  
Slobodan Jergic ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Synthesis ◽  
Genome Stability ◽  
Structural Changes ◽  
Translesion Synthesis ◽  
Dynamic Interaction ◽  
Dna Lesions ◽  
Exonuclease Activity ◽  
Replication Fidelity ◽  
Proper Resolution

DNA lesions stall the replisome and proper resolution of these obstructions is critical for genome stability. Replisomes can directly replicate past a lesion by error-prone translesion synthesis. Alternatively, replisomes can reprime DNA synthesis downstream of the lesion, creating a single-stranded DNA gap that is repaired primarily in an error-free, homology-directed manner. Here we demonstrate how structural changes within theEscherichia colireplisome determine the resolution pathway of lesion-stalled replisomes. This pathway selection is controlled by a dynamic interaction between the proofreading subunit of the replicative polymerase and the processivity clamp, which sets a kinetic barrier to restrict access of translesion synthesis (TLS) polymerases to the primer/template junction. Failure of TLS polymerases to overcome this barrier leads to repriming, which competes kinetically with TLS. Our results demonstrate that independent of its exonuclease activity, the proofreading subunit of the replisome acts as a gatekeeper and influences replication fidelity during the resolution of lesion-stalled replisomes.

Bacteriophage ФX 174

1968 ◽  
Vol 26 ◽  
pp. 32-33
Author(s):  
M. E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nutrient Medium ◽  
Structural Changes ◽  
Uranyl Acetate ◽  
Dense Material ◽  
Medium Ph ◽  
Electron Dense Material ◽  
Virus Particles ◽  
Ultrathin Sections

Cultures of Escherichia coli CIA (Bertani) growing logarithmically in nutrient medium were infected with 5 to 200 bacteriophage §X 174 per cell. At various times after infection the cultures were fixed for 1 hour in nutrient medium containing 5% formaldehyde pH 7, then pelleted and resuspended in 1% OSO4 in L-medium pH 7 for 1 hour; the material was pelleted again and resuspended in a mixture of 1% OsO4 and 1% uranyl-acetate in water; in this mixture the cells were fixed for 10 hours at 20° C; after fixation they were dehydrated in acetone and embedded in Vestopal W. In ultrathin sections the first structural changes became visible 15 minutes after infection when some of the cells seemed to swell and round up. In the cells small aggregates of electron dense material were observed in the chromosomal areas, and sometimes virus particles were also seen within the area of the cells’ chromosome.

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