The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3

2012 ◽  
Vol 97 (11) ◽  
pp. 4849-4858 ◽  
Author(s):  
Jasmina Nikodinovic-Runic ◽  
Lydie Coulombel ◽  
Djordje Francuski ◽  
Narain D. Sharma ◽  
Derek R. Boyd ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Putida ◽  
Wild Type ◽  
Styrene Monooxygenase ◽  
Escherichia Coli Cells

K+ Uptake by Fermenting Escherichia coli Cells: pH Dependent Mode of the TrkA System Operating

2000 ◽  
Vol 20 (4) ◽  
pp. 277-288 ◽  
Author(s):  
Armen Trchounian ◽  
Hiroshi Kobayashi
Keyword(s):  
Escherichia Coli ◽  
Membrane Vesicles ◽  
Wild Type ◽  
K Uptake ◽  
Logarithmic Growth Phase ◽  
E Coli ◽  
Escherichia Coli Cells ◽  
K Concentration ◽  
System Operating ◽  
Logarithmic Growth

Escherichia coli accumulates K+ by means of multiple transportsystems, of which TrkA is the most prominent at neutral and alkalinepH while Kup is major at acidic pH. In the present study, K+ uptakewas observed with cells grown under fermentative conditions at an initialpH of 9.0 and 7.3 (the medium pH decreased to 8.4 and 6.8, respectively, during the mid-logarithmic growth phase), washed with distilled water andresuspended in a K+ containing medium at pH 7.5 in the presence ofglucose. The kinetics for this K+ uptake and the amount of K+accumulated by the wild type and mutants having a functional TrkA or Kup could confirm that K+ uptake by E. coli grown either at pH 9.0or pH 7.3 occurs mainly through TrkA. The following results distinguishpH dependent mode of TrkA operating: (1) K+ uptake was inhibited byDCCD in cells grown either at pH 9.0 or pH 7.3, although the stoichiometryof K+ influx to DCCD-inhibited H+ efflux for bacteria grownat pH 9.0 varied with external K+ concentration, but remained constantfor cells grown at pH 7.3; (2) K+ uptake was observed with an atpDmutant grown at pH 9.0 but not at pH 7.3; (3) The DCCD-inhibited H+efflux was increased 8-fold less by 5 mM K+ added into a K+ freemedium for bacteria grown at pH 9.0 than that for cells grown at pH 7.3;(4) the DCCD-inhibited ATPase activity of membrane vesicles from bacteriagrown at pH 9.0 was reduced a little in the presence of 100 mM K+, but stimulated more than 2.4-fold at pH 7.3.

scholarly journals Genetic Analysis of an Incomplete mutSGene from Pseudomonas putida

2000 ◽  
Vol 182 (18) ◽  
pp. 5278-5279 ◽  
Author(s):  
Yasurou Kurusu ◽  
Tomoaki Narita ◽  
Makoto Suzuki ◽  
Taeko Watanabe
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Genetic Analysis ◽  
Pseudomonas Putida ◽  
Type Strain ◽  
Mutation Frequency ◽  
Wild Type Strain ◽  
Wild Type

ABSTRACT We genetically characterized the Pseudomonas putida mutS gene and found that it encodes a smaller MutS protein than do the genes of other bacteria. This gene is able to function in themutS mutants of Escherichia coli andBacillus subtilis. A P. putida mutS mutant has a mutation frequency 1,000-fold greater than that of the wild-type strain.

Role of UV-inducible proteins in repair of various wild-type Escherichia coli cells

1980 ◽  
Vol 71 (1) ◽  
pp. 15-23 ◽  
Author(s):  
M SEDLIAKOVA ◽  
V SLEZARIKOVA ◽  
J BROZMANOVA ◽  
F MASEK ◽  
V BAYEROVA
Keyword(s):  
Escherichia Coli ◽  
Wild Type ◽  
Escherichia Coli Cells

scholarly journals Colicins, spermine and cephalosporins: a competitive interaction with the OmpF eyelet

2003 ◽  
Vol 376 (1) ◽  
pp. 245-252 ◽  
Author(s):  
Jérôme BREDIN ◽  
Valérie SIMONET ◽  
Ramkumar IYER ◽  
Anne H. DELCOUR ◽  
Jean-Marie PAGÈS
Keyword(s):  
Escherichia Coli ◽  
Structure Function ◽  
Essential Role ◽  
Wild Type ◽  
Potassium Efflux ◽  
Channel Size ◽  
Escherichia Coli Cells ◽  
Epitope Structure ◽  
Resistant Strains ◽  
Kinetics Of

The L3 loop is an important feature of the OmpF porin structure, contributing to both channel size and electrostatic properties. Colicins A and N, spermine, and antibiotics that use OmpF to penetrate the cell, were used to investigate the structure–function relationships of L3. Spermine was found to protect efficiently cells expressing wild-type OmpF from colicin action. Among other solutes, sugars had minor effects on colicin A activity, whereas competitions between colicin A and antibiotic fluxes were observed. Among the antibiotics tested, cefepime appeared the most efficient. Escherichia coli cells expressing various OmpF proteins mutated in the eyelet were tested for their susceptibility to colicin A, and resistant strains were found only among L3 mutants. Mutations at residues 119 and 120 were the most effective at conferring resistance to colicin A, probably due to epitope structure alteration, as revealed by a specific antipeptide. More detailed information was obtained on mutants D113A and D121A, by focusing on the kinetics of colicin A and colicin N activities through measurements of potassium efflux. D113 appeared to play an essential role for colicin A activity, whereas colicin N activity was more dependent on D121 than on D113.

scholarly journals The initiation cascade for chromosome replication in wild-type and Dam methyltransferase deficient Escherichia coli cells.

1994 ◽  
Vol 13 (8) ◽  
pp. 1856-1862 ◽  
Author(s):  
A. Løbner-Olesen ◽  
F.G. Hansen ◽  
K.V. Rasmussen ◽  
B. Martin ◽  
P.L. Kuempel
Keyword(s):  
Escherichia Coli ◽  
Chromosome Replication ◽  
Wild Type ◽  
Escherichia Coli Cells

scholarly journals Presence of Multiple Sites Containing Polar Material in Spherical Escherichia coli Cells That Lack MreB

2005 ◽  
Vol 187 (17) ◽  
pp. 6187-6196 ◽  
Author(s):  
Trine Nilsen ◽  
Arthur W. Yan ◽  
Gregory Gale ◽  
Marcia B. Goldberg
Keyword(s):  
Escherichia Coli ◽  
Fluorescent Protein ◽  
Positional Information ◽  
Actin Assembly ◽  
Wild Type ◽  
Polar Material ◽  
Transposon Insertion ◽  
Escherichia Coli Cells ◽  
Inner Membrane Protein ◽  
Green Fluorescent

ABSTRACT In rod-shaped bacteria, certain proteins are specifically localized to the cell poles. The nature of the positional information that leads to the proper localization of these proteins is unclear. In a screen for factors required for the localization of the Shigella sp. actin assembly protein IcsA to the bacterial pole, a mutant carrying a transposon insertion in mreB displayed altered targeting of IcsA. The phenotype of cells containing a transposon insertion in mreB was indistinguishable from that of cells containing a nonpolar mutation in mreB or that of wild-type cells treated with the MreB inhibitor A22. In cells lacking MreB, a green fluorescent protein (GFP) fusion to a cytoplasmic derivative of IcsA localized to multiple sites. Secreted full-length native IcsA was present in multiple faint patches on the surfaces of these cells in a pattern similar to that seen for the cytoplasmic IcsA-GFP fusion. EpsM, the polar Vibrio cholerae inner membrane protein, also localized to multiple sites in mreB cells and colocalized with IcsA, indicating that localization to multiple sites is not unique to IcsA. Our results are consistent with the requirement, either direct or indirect, for MreB in the restriction of certain polar material to defined sites within the cell and, in the absence of MreB, with the formation of ectopic sites containing polar material.

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