Transcriptional analysis reveals the critical role of RNA polymerase-binding transcription factor, DksA, in regulating multi-drug resistance of Escherichia coli

2018 ◽  
Vol 52 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Jiawei Wang ◽  
Li Cao ◽  
Xiaowen Yang ◽  
Qingmin Wu ◽  
Lin Lu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Drug Resistance ◽  
Transcription Factor ◽  
Rna Polymerase ◽  
Critical Role ◽  
Transcriptional Analysis ◽  
Multi Drug Resistance ◽  
Polymerase Binding

scholarly journals The hydrophobic heptad repeat in Region III of Escherichia coli transcription factor sigma 54 is essential for core RNA polymerase binding

Microbiology ◽  
1999 ◽  
Vol 145 (11) ◽  
pp. 3081-3088 ◽  
Author(s):  
Mingli Hsieh ◽  
Hsiu-Mei Hsu ◽  
Shiow-Fen Hwang ◽  
Feng-Chen Wen ◽  
Ju-Shan Yu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Rna Polymerase ◽  
Heptad Repeat ◽  
Sigma 54 ◽  
Polymerase Binding

scholarly journals Escherichia Coli Isolate From Hospital Sewage Is Carrying blaNDM-1 and blaoxa-10

2021 ◽  
Author(s):  
Zimeng Hu ◽  
Weiye Chen ◽  
Genglin Guo ◽  
Chen Dong ◽  
Yun Shen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Drug Resistance ◽  
Hospital Environment ◽  
Multi Drug Resistance ◽  
Resistant Bacteria ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Drug Resistant Bacteria ◽  
Hospital Sewage

Abstract Carbapenems, as the “last line of defense” against gram-negative bacteria, are increasingly being challenged by drug-resistant bacteria, especially in Enterobacteriaceae. In this study, a carbapenems resistant gram-negative bacterium, named AH001, was isolated from hospital sewage, and modified Hoge test confirmed this bacterium can produce carbapenemase. Further analysis revealed that this bacterium is multi-drug resistance, which against additional seven antibiotics. Whole-genome sequencing and analysis showed that AH001 could not be classified by existing MLST, and its serotype couldn’t be distinguished among O9, O89 or O168 in O antigen prediction. More attention should be paid to the role of environmental source Escherichia coli in the development and transfer of drug resistance in the hospital environment.

scholarly journals Probing Zn2+-binding effects on the zinc-ribbon domain of human general transcription factor TFIIB

2004 ◽  
Vol 378 (2) ◽  
pp. 317-324 ◽  
Author(s):  
Mahua GHOSH ◽  
Laura M. ELSBY ◽  
Tapas K. MAL ◽  
Jane M. GOODING ◽  
Stefan G. E. ROBERTS ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Structural Changes ◽  
Core Promoter ◽  
Critical Role ◽  
General Transcription Factor ◽  
Structural Rigidity ◽  
Zinc Ribbon

The general transcription factor, TFIIB, plays an important role in the assembly of the pre-initiation complex. The N-terminal domain (NTD) of TFIIB contains a zinc-ribbon motif, which is responsible for the recruitment of RNA polymerase II and TFIIF to the core promoter region. Although zinc-ribbon motif structures of eukaryotic and archaeal TFIIBs have been reported previously, the structural role of Zn2+ binding to TFIIB remains to be determined. In the present paper, we report NMR and biochemical studies of human TFIIB NTD, which characterize the structure and dynamics of the TFIIB Zn2+-binding domain in both Zn2+-bound and -free states. The NMR data show that, whereas the backbone fold of NTD is pre-formed in the apo state, Zn2+ binding reduces backbone mobility in the β-turn (Arg28–Gly30), induces enhanced structural rigidity of the charged-cluster domain in the central linker region of TFIIB and appends a positive surface charge within the Zn2+-binding site. V8 protease-sensitivity assays of full-length TFIIB support the Zn2+-dependent structural changes. These structural effects of Zn2+ binding on TFIIB may have a critical role in interactions with its binding partners, such as the Rpb1 subunit of RNA polymerase II.

scholarly journals Role of the AraC–XylS family regulator YdeO in multi-drug resistance of Escherichia coli

2009 ◽  
Vol 62 (5) ◽  
pp. 251-257 ◽  
Author(s):  
Kunihiko Nishino ◽  
Yasuko Senda ◽  
Mitsuko Hayashi-Nishino ◽  
Akihito Yamaguchi
Keyword(s):  
Escherichia Coli ◽  
Drug Resistance ◽  
Multi Drug Resistance

scholarly journals Activation and Repression at the Escherichia coli ynfEFGHI Operon Promoter

2009 ◽  
Vol 191 (9) ◽  
pp. 3172-3176 ◽  
Author(s):  
Meng Xu ◽  
Stephen J. W. Busby ◽  
Douglas F. Browning
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Rna Polymerase ◽  
Class Ii ◽  
Nitrate Ions ◽  
Single Target ◽  
Promoter Complex ◽  
Polymerase Binding ◽  
K 12 ◽  
Rna Polymerase Promoter

ABSTRACT Induction of the Escherichia coli K-12 ynfEFGHI operon in response to anaerobiosis is repressed by nitrate ions. In this study, we show that the global transcription factor FNR is a class II activator at the ynfEFGHI promoter and that NarL represses activation by binding to a single target that overlaps the promoter −10 element. Electromobility shift assays show that NarL does not prevent RNA polymerase binding and suggest that repression may involve a quaternary NarL-FNR-RNA polymerase-promoter complex.

scholarly journals A critical role of autocrine sonic hedgehog signaling in human CD138+ myeloma cell survival and drug resistance

Blood ◽  
2014 ◽  
Vol 124 (13) ◽  
pp. 2061-2071 ◽  
Author(s):  
Zhiqiang Liu ◽  
Jingda Xu ◽  
Jin He ◽  
Yuhuan Zheng ◽  
Haiyan Li ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Cell Survival ◽  
Sonic Hedgehog ◽  
Hedgehog Signaling ◽  
Critical Role ◽  
Myeloma Cell ◽  
Sonic Hedgehog Signaling ◽  
Key Points

Key Points CD138+ MM cells are a major source of SHH. Autocrine SHH enhances MM drug resistance.

SATP (YaaH), a succinate–acetate transporter protein in Escherichia coli

2013 ◽  
Vol 454 (3) ◽  
pp. 585-595 ◽  
Author(s):  
Joana Sá-Pessoa ◽  
Sandra Paiva ◽  
David Ribas ◽  
Inês Jesus Silva ◽  
Sandra Cristina Viegas ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acetic Acid ◽  
Succinic Acid ◽  
Critical Role ◽  
Amino Acid Residues ◽  
E Coli ◽  
Transporter Protein ◽  
Affinity Constants ◽  
In Trans

In the present paper we describe a new carboxylic acid transporter in Escherichia coli encoded by the gene yaaH. In contrast to what had been described for other YaaH family members, the E. coli transporter is highly specific for acetic acid (a monocarboxylate) and for succinic acid (a dicarboxylate), with affinity constants at pH 6.0 of 1.24±0.13 mM for acetic acid and 1.18±0.10 mM for succinic acid. In glucose-grown cells the ΔyaaH mutant is compromised for the uptake of both labelled acetic and succinic acids. YaaH, together with ActP, described previously as an acetate transporter, affect the use of acetic acid as sole carbon and energy source. Both genes have to be deleted simultaneously to abolish acetate transport. The uptake of acetate and succinate was restored when yaaH was expressed in trans in ΔyaaH ΔactP cells. We also demonstrate the critical role of YaaH amino acid residues Leu131 and Ala164 on the enhanced ability to transport lactate. Owing to its functional role in acetate and succinate uptake we propose its assignment as SatP: the Succinate–Acetate Transporter Protein.

scholarly journals Autocrine IL-6/STAT3 signaling aids development of acquired drug resistance in Group 3 medulloblastoma

2020 ◽  
Vol 11 (12) ◽  
Author(s):  
Lakshana Sreenivasan ◽  
Hui Wang ◽  
Shyong Quin Yap ◽  
Pascal Leclair ◽  
Anthony Tam ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Multi Drug Resistance ◽  
Acquired Drug Resistance ◽  
Stat3 Signaling ◽  
Therapeutic Benefits ◽  
Signaling Axis ◽  
Neuronal Precursors ◽  
Cranial Fossa ◽  
Group 3

AbstractMedulloblastoma (MB) is a high-grade pediatric brain malignancy that originates from neuronal precursors located in the posterior cranial fossa. In this study, we evaluated the role of STAT3 and IL-6 in a tumor microenvironment mediated drug resistance in human MBs. We established that the Group 3 MB cell line, Med8A, is chemosensitive (hence Med8A-S), and this is correlated with a basal low phosphorylated state of STAT3, while treatment with IL-6 induced robust increases in pY705-STAT3. Via incremental selection with vincristine, we derived the stably chemoresistant variant, Med8A-R, that exhibited multi-drug resistance, enhanced IL-6 induced pY705-STAT3 levels, and increased IL6R expression. Consequently, abrogation of STAT3 or IL6R expression in Med8A-R led to restored chemosensitivity to vincristine, highlighting a prominent role for canonical IL-6/STAT3 signaling in acquired drug resistance. Furthermore, Med8A-S subjected to conditioning exposure with IL-6, termed Med8A-IL6+ cells, exhibited enhanced vincristine resistance, increased expression of pY705-STAT3 and IL6R, and increased secretion of IL-6. When cocultured with Med8A-IL6+ cells, Med8A-S cells exhibited increased pY705-STAT3 and increased IL-6 secretion, suggesting a cytokine feedback loop responsible for amplifying STAT3 activity. Similar IL-6 induced phenomena were also observed in the Group 3 MB cell lines, D283 and D341, including increased pY705-STAT3, drug resistance, IL-6 secretion and IL6R expression. Our study unveiled autocrine IL-6 as a promoter of STAT3 signaling in development of drug resistance, and suggests therapeutic benefits for targeting the IL-6/STAT3 signaling axis in Group 3 MBs.

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