scholarly journals Studies on the sequence and structure of the Escherichia coli K-12 nupG gene, encoding a nucleoside-transport system

1987 ◽  
Vol 168 (2) ◽  
pp. 385-391 ◽  
Author(s):  
Svend Erik WESTH HANSEN ◽  
Nina JENSEN ◽  
Agnete MUNCH-PETERSEN
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
Nucleoside Transport ◽  
Gene Encoding ◽  
K 12

scholarly journals Novel regulators of the csgD gene encoding the master regulator of biofilm formation in Escherichia coli K-12

Microbiology ◽  
2020 ◽  
Vol 166 (9) ◽  
pp. 880-890 ◽  
Author(s):  
Hiroshi Ogasawara ◽  
Toshiyuki Ishizuka ◽  
Shuhei Hotta ◽  
Michiko Aoki ◽  
Tomohiro Shimada ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biofilm Formation ◽  
Cell Aggregation ◽  
Master Regulator ◽  
Gene Encoding ◽  
Content Type ◽  
Promoter Probe ◽  
K 12 ◽  
Specific Environmental Condition

Under stressful conditions, Escherichia coli forms biofilm for survival by sensing a variety of environmental conditions. CsgD, the master regulator of biofilm formation, controls cell aggregation by directly regulating the synthesis of Curli fimbriae. In agreement of its regulatory role, as many as 14 transcription factors (TFs) have so far been identified to participate in regulation of the csgD promoter, each monitoring a specific environmental condition or factor. In order to identify the whole set of TFs involved in this typical multi-factor promoter, we performed in this study ‘promoter-specific transcription-factor’ (PS-TF) screening in vitro using a set of 198 purified TFs (145 TFs with known functions and 53 hitherto uncharacterized TFs). A total of 48 TFs with strong binding to the csgD promoter probe were identified, including 35 known TFs and 13 uncharacterized TFs, referred to as Y-TFs. As an attempt to search for novel regulators, in this study we first analysed a total of seven Y-TFs, including YbiH, YdcI, YhjC, YiaJ, YiaU, YjgJ and YjiR. After analysis of curli fimbriae formation, LacZ-reporter assay, Northern-blot analysis and biofilm formation assay, we identified at least two novel regulators, repressor YiaJ (renamed PlaR) and activator YhjC (renamed RcdB), of the csgD promoter.

scholarly journals Characterization of the specific pyruvate transport system in Escherichia coli K-12.

1987 ◽  
Vol 169 (1) ◽  
pp. 380-385 ◽  
Author(s):  
V J Lang ◽  
C Leystra-Lantz ◽  
R A Cook
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
K 12

scholarly journals Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12.

1988 ◽  
Vol 170 (12) ◽  
pp. 5901-5907 ◽  
Author(s):  
R Lahti ◽  
T Pitkäranta ◽  
E Valve ◽  
I Ilta ◽  
E Kukko-Kalske ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Inorganic Pyrophosphatase ◽  
Gene Encoding ◽  
K 12

scholarly journals Genetic Evidence for an Interaction of the UbiG O-Methyltransferase with UbiX in Escherichia coli Coenzyme Q Biosynthesis

2006 ◽  
Vol 188 (17) ◽  
pp. 6435-6439 ◽  
Author(s):  
Melissa Gulmezian ◽  
Haitao Zhang ◽  
George T. Javor ◽  
Catherine F. Clarke
Keyword(s):  
Escherichia Coli ◽  
Mutant Strain ◽  
Coenzyme Q ◽  
Genetic Evidence ◽  
Deficient Mutant ◽  
Gene Encoding ◽  
K 12

ABSTRACT IS16 is a thiol-sensitive, Q-deficient mutant strain of Escherichia coli. Here, we show that IS16 harbors a mutation in the ubiG gene encoding a methyltransferase required for two O-methylation steps of Q biosynthesis. Complementation of IS16 with either ubiG or ubiX K-12 reverses this phenotype, suggesting that UbiX may interact with UbiG.

scholarly journals Purification and properties of uroporphyrinogen III synthase (co-synthase) from an overproducing recombinant strain of Escherichia coli K-12

1989 ◽  
Vol 264 (2) ◽  
pp. 397-402 ◽  
Author(s):  
A F Alwan ◽  
B I A Mgbeje ◽  
P M Jordan
Keyword(s):  
Escherichia Coli ◽  
Specific Activity ◽  
Heat Inactivation ◽  
Gene Encoding ◽  
Ph Optimum ◽  
Nitrobenzoic Acid ◽  
Purification And Properties ◽  
Lower Reactivity ◽  
In The Wild ◽  
K 12

The Escherichia coli hemD gene, encoding the enzyme uroporphyrinogen III synthase (co-synthase), was cloned into multi-copy plasmids in E. coli cells that were used to generate strains producing up to 1000 times the concentration of the synthase in the wild-type. The enzyme was purified to homogeneity from these strains in milligram amounts. The enzyme is a monomer of Mr 28,000 with an isoelectric point of 5.2 and a pH optimum of 7.8. The specific activity of the purified synthase is 1500 units/mg and the Km for the substrate, pre-uroporphyrinogen, is 5 microM. The N-terminal sequence of the enzyme is Ser-Ile-Leu-Val-Thr-Arg-Pro-Ser-Pro-Ala-Gly-, in agreement with the gene-derived protein sequence. The enzyme contains four 5,5′-dithiobis-(2-nitrobenzoic acid)-titratable groups, one reacting rapidly with the reagent and three further groups having lower reactivity. The enzyme is heat-sensitive, and during heat inactivation all four thiol groups become equally available for reaction.

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