scholarly journals The PaaX Repressor, a Link between Penicillin G Acylase and the Phenylacetyl-Coenzyme A Catabolon of Escherichia coli W

2004 ◽  
Vol 186 (7) ◽  
pp. 2215-2220 ◽  
Author(s):  
Beatriz Galán ◽  
José L. García ◽  
María A. Prieto
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Regulatory Mechanism ◽  
Penicillin G Acylase ◽  
Receptor Protein ◽  
Penicillin G ◽  
Catabolic Pathway ◽  
Gene Encoding ◽  
Unusual Position

ABSTRACT The pac gene, encoding the penicillin G acylase from Escherichia coli W, is regulated by the PaaX repressor of the phenylacetate catabolic pathway. pac expression depends on the synthesis of phenylacetyl-coenzyme A. PaaX and the cyclic AMP receptor protein (CRP) bind in vitro to the Ppac promoter region. A palindromic sequence proposed as the PaaX operator is located upstream of the −35 box overlapping a CRP binding site, an unusual position that suggests a novel regulatory mechanism.

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 Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli.

1986 ◽  
Vol 168 (1) ◽  
pp. 431-433 ◽  
Author(s):  
G O Daumy ◽  
J A Williams ◽  
A S McColl ◽  
T J Zuzel ◽  
D Danley
Keyword(s):  
Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G

scholarly journals Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus

2001 ◽  
Vol 183 (17) ◽  
pp. 5198-5202 ◽  
Author(s):  
Pongpan Laksanalamai ◽  
Dennis L. Maeder ◽  
Frank T. Robb
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mechanism Of Action ◽  
Pyrococcus Furiosus ◽  
Small Heat Shock Protein ◽  
Control Culture ◽  
Gene Encoding ◽  
E Coli

ABSTRACT The small heat shock protein (sHSP) from the hyperthermophilePyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. colioverexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

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