Co-dependent positive regulation of the ansBF promoter of Escherichia coli by CRP and the FNR protein: a molecular analysis

1993 ◽  
Vol 9 (1) ◽  
pp. 155-164 ◽  
Author(s):  
Michael P. Jennings ◽  
Ifor R. Beacham
Keyword(s):  
Escherichia Coli ◽  
Molecular Analysis ◽  
Protein A ◽  
Positive Regulation ◽  
Fnr Protein

scholarly journals Fnr Is Involved in Oxygen Control of Herbaspirillum seropedicae N-Truncated NifA Protein Activity in Escherichia coli

2003 ◽  
Vol 69 (3) ◽  
pp. 1527-1531 ◽  
Author(s):  
Rose A. Monteiro ◽  
Emanuel M. de Souza ◽  
M. Geoffrey Yates ◽  
Fabio O. Pedrosa ◽  
Leda S. Chubatsu
Keyword(s):  
Escherichia Coli ◽  
Protein A ◽  
Ammonium Ions ◽  
Oxygen Control ◽  
Herbaspirillum Seropedicae ◽  
Protein Activity ◽  
Iron Deprivation ◽  
Iron Requirement ◽  
Fnr Protein ◽  
Nifa Protein

ABSTRACT Herbaspirillum seropedicae is an endophytic diazotroph belonging to the β-subclass of the class Proteobacteria, which colonizes many members of the Gramineae. The activity of the NifA protein, a transcriptional activator of nif genes in H. seropedicae, is controlled by ammonium ions through its N-terminal domain and by oxygen through mechanisms that are not well understood. Here we report that the NifA protein of H. seropedicae is inactive and more susceptible to degradation in an fnr Escherichia coli background. Both effects correlate with oxygen exposure and iron deprivation. Our results suggest that the oxygen sensitivity and iron requirement for H. seropedicae NifA activity involve the Fnr protein.

Overexpression of Outer Membrane Protein A Is a Risk Factor for Mortality in Escherichia coli Bloodstream Infections

2019 ◽  
Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Risk Factor ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Bloodstream Infections ◽  
Outer Membrane Protein A

Molecular analysis of the U2 snRNP unique protein A?

1987 ◽  
Vol 12 (3) ◽  
pp. 155-155
Author(s):  
Lucille D. Fresco ◽  
Jack D. Keene
Keyword(s):  
Molecular Analysis ◽  
Protein A ◽  
Unique Protein ◽  
U2 Snrnp

scholarly journals Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli

2001 ◽  
Vol 40 (1) ◽  
pp. 245-256 ◽  
Author(s):  
Bangdong L. Wei ◽  
Anne-Marie Brun-Zinkernagel ◽  
Jerry W. Simecka ◽  
Birgit M. Prüß ◽  
Paul Babitzke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Positive Regulation

scholarly journals Recombinant outer membrane protein A fragments protect against Escherichia coli meningitis

2016 ◽  
Vol 49 (3) ◽  
pp. 329-334 ◽  
Author(s):  
Wen-Shyang Hsieh ◽  
Yi-Yuan Yang ◽  
Hsin-Yi Yang ◽  
Yu-Shan Huang ◽  
Hsueh-Hsia Wu
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Outer Membrane Protein A

Molecular characterization of three mutations in katG affecting the activity of hydroperoxidase I of Escherichia coli

1990 ◽  
Vol 68 (7-8) ◽  
pp. 1037-1044 ◽  
Author(s):  
Peter C. Loewen ◽  
Jacek Switala ◽  
Mark Smolenski ◽  
Barbara L. Triggs-Raine
Keyword(s):  
Escherichia Coli ◽  
Specific Activity ◽  
Polymerase Chain Reaction Amplification ◽  
Protein A ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Gene Encoding ◽  
Reaction Amplification ◽  
Mutant Genes

Hydroperoxidase I (HPI) of Escherichia coli is a bifunctional enzyme exhibiting both catalase and peroxidase activities. Mutants lacking appreciable HPI have been generated using nitrosoguanidine and the gene encoding HPI, katG, has been cloned from three of these mutants using either classical probing methods or polymerase chain reaction amplification. The mutant genes were sequenced and the changes from wild-type sequence identified. Two mutants contained G to A changes in the coding strand, resulting in glycine to aspartate changes at residues 119 (katG15) and 314 (katG16) in the deduced amino acid sequence of the protein. A third mutant contained a C to T change resulting in a leucine to phenylalanine change at residue 139 (katG14). The Phe139-, Asp119-, and Asp314-containing mutants exhibited 13, < 1, and 18%, respectively, of the wild-type catalase specific activity and 43, 4, and 45% of the wild-type peroxidase specific activity. All mutant enzymes bound less protoheme IX than the wild-type enzyme. The sensitivities of the mutant enzymes to the inhibitors hydroxylamine, azide, and cyanide and the activators imidazole and Tris were similar to those of the wild-type enzyme. The mutant enzymes were more sensitive to high temperature and to β-mercaptoethanol than the wild-type enzyme. The pH profiles of the mutant catalases were unchanged from the wild-type enzyme.Key words: catalase, hydroperoxidase I, mutants, sequence analysis.

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