scholarly journals Effects of the Escherichia coli sfsA Gene on mal Genes Expression and a DNA Binding Activity of SfsA

2001 ◽  
Vol 65 (1) ◽  
pp. 213-217 ◽  
Author(s):  
Kazuhiko TAKEDA ◽  
Chiyuri AKIMOTO ◽  
Makoto KAWAMUKAI
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Genes Expression ◽  
Mal Genes

scholarly journals Specific DNA Binding and Regulation of Its Own Expression by the AidB Protein in Escherichia coli

2010 ◽  
Vol 192 (23) ◽  
pp. 6136-6142 ◽  
Author(s):  
Valentina Rippa ◽  
Angela Amoresano ◽  
Carla Esposito ◽  
Paolo Landini ◽  
Michael Volkert ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Alkylating Agents ◽  
Specific Interaction ◽  
Domain Architecture ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Preferential Binding

ABSTRACT Upon exposure to alkylating agents, Escherichia coli increases expression of aidB along with three genes (ada, alkA, and alkB) that encode DNA repair proteins. While the biological roles of the Ada, AlkA, and AlkB proteins have been defined, despite many efforts, the molecular functions of AidB remain largely unknown. In this study, we focused on the biological role of the AidB protein, and we demonstrated that AidB shows preferential binding to a DNA region that includes the upstream element of its own promoter, PaidB. The physiological significance of this specific interaction was investigated by in vivo gene expression assays, demonstrating that AidB can repress its own synthesis during normal cell growth. We also showed that the domain architecture of AidB is related to the different functions of the protein: the N-terminal region, comprising the first 439 amino acids (AidB “I-III”), possesses FAD-dependent dehydrogenase activity, while its C-terminal domain, corresponding to residues 440 to 541 (AidB “IV”), displays DNA binding activity and can negatively regulate the expression of its own gene in vivo. Our results define a novel role in gene regulation for the AidB protein and underline its multifunctional nature.

scholarly journals Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity

1996 ◽  
Vol 143 (2-3) ◽  
pp. 211-216 ◽  
Author(s):  
Abu Z.M. Saleh ◽  
Kunitoshi Yamanaka ◽  
Hironori Niki ◽  
Teru Ogura ◽  
Mitsuyoshi Yamazoe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Activity ◽  
Terminal Region ◽  
Dna Binding Activity ◽  
Carboxyl Terminal

scholarly journals Enterohemorrhagic Escherichia coli Infection Induces Interleukin-8 Production via Activation of Mitogen-Activated Protein Kinases and the Transcription Factors NF-κB and AP-1 in T84 Cells

2002 ◽  
Vol 70 (5) ◽  
pp. 2304-2310 ◽  
Author(s):  
Stephanie Dahan ◽  
Valere Busuttil ◽  
Veronique Imbert ◽  
Jean-Francois Peyron ◽  
Patrick Rampal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Transcription Factors ◽  
Dna Binding ◽  
Protein Kinases ◽  
Binding Activity ◽  
Interleukin 8 ◽  
T84 Cells ◽  
Mitogen Activated Protein Kinases ◽  
Dna Binding Activity ◽  
Mitogen Activated Protein

ABSTRACT Enterohemorrhagic Escherichia coli (EHEC) infections are associated with hemorrhagic colitis and the hemolytic-uremic syndrome (HUS). In vivo, elevated plasma levels of the proinflammatory cytokine interleukin-8 (IL-8) in EHEC-infected children are correlated with a high risk of developing HUS. As IL-8 gene transcription is regulated by the transcription factors NF-κB and AP-1, we analyzed the role of these factors in the regulation of IL-8 production after infection of the epithelial intestinal T84 cell line by EHEC. By 6 h of infection, EHEC had induced significant secretion of IL-8 (35.84 ± 6.76 ng/ml versus 0.44 ± 0.04 ng/ml in control cells). EHEC induced AP-1 and NF-κB activation by 3 h of infection. Moreover, the three mitogen-activated protein kinases (MAPK) (ERK1/2, p38, and JNK) were phosphorylated in EHEC-infected T84 cells concomitant with induction of AP-1 DNA binding activity, and IκB-α was phosphorylated and then degraded concomitant with induction of NF-κB DNA binding activity. Pretreatment of cells with the highly specific MEK1/2 inhibitor U0126, the p38 inhibitor SB203580, and/or the proteasome inhibitor ALLN led to inhibition of the IL-8 secretion induced in EHEC-infected T84 cells. These findings demonstrate that (i) EHEC can induce in vitro a potent proinflammatory response by secretion of IL-8 and (ii) the secretion of IL-8 is due to the involvement of MAPK, AP-1, and NF-κB signaling pathways.

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