Aspects on Structure and Function of Pili on Uropathogenic Escherichia coli

2015 ◽  
pp. 189-202
Author(s):  
C. Svanborg Ed�n ◽  
E. C. Gotschlich ◽  
T. K. Korhonen ◽  
H. Leffler ◽  
G. Schoolnik
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
Uropathogenic Escherichia Coli ◽  
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.

scholarly journals Influence of High Pressure on the Dimerization of ToxR, a Protein Involved in Bacterial Signal Transduction

2008 ◽  
Vol 74 (24) ◽  
pp. 7821-7823 ◽  
Author(s):  
Kai Linke ◽  
Nagarajan Periasamy ◽  
Matthias Ehrmann ◽  
Roland Winter ◽  
Rudi F. Vogel
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
High Pressure ◽  
Structure And Function ◽  
Transmembrane Segments ◽  
Bacterial Signal Transduction ◽  
Reporter Strains ◽  
And Function ◽  
First Time

ABSTRACT High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.

scholarly journals The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit.

1993 ◽  
Vol 268 (36) ◽  
pp. 27094-27099
Author(s):  
B Stolz ◽  
M Huber ◽  
Z Marković-Housley ◽  
B Erni
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
And Function

1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function

2007 ◽  
Vol 1 (1) ◽  
pp. 89-91 ◽  
Author(s):  
Julien Boudet ◽  
Anne Chouquet ◽  
Aicha Chahboune ◽  
Cécile Giustini ◽  
Bernard Joris ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Resonance Assignments ◽  
Structure And Function ◽  
Unknown Structure ◽  
And Function

STRUCTURE AND FUNCTION OF ESCHERICHIA COLI RIBOSOME

1981 ◽  
pp. 417-428
Author(s):  
D.P. BURMA ◽  
S. SINHARAY ◽  
D. CHATTERJI ◽  
Z. ALI ◽  
M. DAS ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
And Function

Frank William Ernest Gibson 1923 - 2008

2010 ◽  
Vol 21 (1) ◽  
pp. 55 ◽  
Author(s):  
A. J. Pittard ◽  
G. B. Cox
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Genetic Analysis ◽  
Aromatic Compounds ◽  
Aromatic Amino Acids ◽  
Atp Synthesis ◽  
Structure And Function ◽  
Innovative Model ◽  
Distinguished Research ◽  
And Function

Frank Gibson died in Canberra on 11 July 2008. Frank was a highly distinguished research scientist who will be remembered for his pioneering studies in identifying the branch-point compound in the pathway of biosynthesis of a large number of important aromatic compounds followed by a detailed biochemical and genetic analysis of many of the pathways leading to the aromatic amino acids and the so-called aromatic vitamins. Studies on ubiquinone synthesis and function led to an examination of oxidative phosphorylation and the structure and function of the F1F0-ATPase in the bacterium Escherichia coli. This work resulted in the formulation of a highly innovative model, involving rotating subunits of the F0 segment within the membrane and offering an explanation for the mechanism linking proton flow and ATP synthesis.

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