Structure and function of the conserved 690 hairpin in Escherichia coli 16 s ribosomal RNA. II. NMR solution structure

2001 ◽  
Vol 307 (1) ◽  
pp. 197-211 ◽  
Author(s):  
Svetlana V. Morosyuk ◽  
Philip R. Cunningham ◽  
John SantaLucia
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Solution Structure ◽  
Structure And Function ◽  
Nmr Solution Structure ◽  
And Function

scholarly journals NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor

FEBS Journal ◽  
2010 ◽  
Vol 277 (12) ◽  
pp. 2611-2627 ◽  
Author(s):  
Alexey B. Mantsyzov ◽  
Elena V. Ivanova ◽  
Berry Birdsall ◽  
Elena Z. Alkalaeva ◽  
Polina N. Kryuchkova ◽  
...  
Keyword(s):  
Solution Structure ◽  
Polypeptide Chain ◽  
Structure And Function ◽  
Release Factor ◽  
Nmr Solution Structure ◽  
Terminal Domain ◽  
Class 1 ◽  
And Function

Structure and function of the conserved 690 hairpin in Escherichia coli 16 s ribosomal RNA: analysis of the stem nucleotides

2000 ◽  
Vol 300 (1) ◽  
pp. 113-126 ◽  
Author(s):  
Svetlana V Morosyuk ◽  
KangSeok Lee ◽  
John SantaLucia ◽  
Philip R Cunningham
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Structure And Function ◽  
Rna Analysis ◽  
And Function

scholarly journals Micro-analysis of pure deoxyribonucleic acid-dependent ribonucleic acid polymerase from Escherichia coli. Action of heparin and rifampicin on structure and function

1970 ◽  
Vol 117 (3) ◽  
pp. 623-631 ◽  
Author(s):  
Volker Neuhoff ◽  
Wolf-Bernhard Schill ◽  
Hans Sternbach
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rna Synthesis ◽  
Deoxyribonucleic Acid ◽  
Structure And Function ◽  
Disc Electrophoresis ◽  
Inhibitory Mechanism ◽  
And Function ◽  
Micro Analysis ◽  
Template Complex

By using micro disc electrophoresis and micro-diffusion techniques, the interaction of pure DNA-dependent RNA polymerase (EC 2.7.7.6) from Escherichia coli with the template, the substrates and the inhibitors heparin and rifampicin was investigated. The following findings were obtained: (1) heparin converts the 24S and 18S particles of the polymerase into the 13S form; (2) heparin inhibits RNA synthesis by dissociating the enzyme–template complex; (3) rifampicin does not affect the attachment of heparin to the enzyme; (4) the substrates ATP and UTP are bound by enzyme loaded with rifampicin; (5) rifampicin is bound by an enzyme–template complex to the same extent as by an RNA-synthesizing enzyme–template complex. From this it is concluded that the mechanism of the inhibition of RNA synthesis by rifampicin is radically different from that by heparin. As a working hypothesis to explain the inhibitory mechanism of rifampicin, it is assumed that it becomes very firmly attached to a position close to the synthesizing site and only blocks this when no synthesis is in progress.

Studies on the structure and function of 16S ribosomal RNA using structure-specific chemical probes

1985 ◽  
Vol 8 (3-4) ◽  
pp. 747-755 ◽  
Author(s):  
Harry F. Noller ◽  
Barbara J. Van Stolk ◽  
Danesh Moazed ◽  
Stephen Douthwaite ◽  
Robin R. Gutell
Keyword(s):  
Ribosomal Rna ◽  
Structure And Function ◽  
16S Ribosomal Rna ◽  
Chemical Probes ◽  
Specific Chemical ◽  
And Function
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