scholarly journals Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli

2001 ◽  
Vol 40 (1) ◽  
pp. 245-256 ◽  
Author(s):  
Bangdong L. Wei ◽  
Anne-Marie Brun-Zinkernagel ◽  
Jerry W. Simecka ◽  
Birgit M. Prüß ◽  
Paul Babitzke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Positive Regulation

scholarly journals Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ

2020 ◽  
Vol 48 (8) ◽  
pp. 4507-4520 ◽  
Author(s):  
Smriti Pandey ◽  
Chandra M Gravel ◽  
Oliver M Stockert ◽  
Clara D Wang ◽  
Courtney L Hegner ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Mechanisms ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Site Directed Mutagenesis ◽  
Genetic Identification ◽  
Messenger Rnas ◽  
Functional Surface

Abstract The FinO-domain-protein ProQ is an RNA-binding protein that has been known to play a role in osmoregulation in proteobacteria. Recently, ProQ has been shown to act as a global RNA-binding protein in Salmonella and Escherichia coli, binding to dozens of small RNAs (sRNAs) and messenger RNAs (mRNAs) to regulate mRNA-expression levels through interactions with both 5′ and 3′ untranslated regions (UTRs). Despite excitement around ProQ as a novel global RNA-binding protein, and its potential to serve as a matchmaking RNA chaperone, significant gaps remain in our understanding of the molecular mechanisms ProQ uses to interact with RNA. In order to apply the tools of molecular genetics to this question, we have adapted a bacterial three-hybrid (B3H) assay to detect ProQ’s interactions with target RNAs. Using domain truncations, site-directed mutagenesis and an unbiased forward genetic screen, we have identified a group of highly conserved residues on ProQ’s NTD as the primary face for in vivo recognition of two RNAs, and propose that the NTD structure serves as an electrostatic scaffold to recognize the shape of an RNA duplex.

scholarly journals Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein

1998 ◽  
Vol 17 (14) ◽  
pp. 4092-4100 ◽  
Author(s):  
Martin Huenges ◽  
Christian Rölz ◽  
Ruth Gschwind ◽  
Ralph Peteranderl ◽  
Fabian Berglechner ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Solution Structure ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA-binding protein Hfq assembles into foci-like structures in nitrogen starved Escherichia coli

2020 ◽  
Vol 295 (35) ◽  
pp. 12355-12367
Author(s):  
Josh McQuail ◽  
Amy Switzer ◽  
Lynn Burchell ◽  
Sivaramesh Wigneshweraraj
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Adaptive Response ◽  
Rna Binding ◽  
Nitrogen Starvation ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Rna Binding Protein ◽  
E Coli

The initial adaptive responses to nutrient depletion in bacteria often occur at the level of gene expression. Hfq is an RNA-binding protein present in diverse bacterial lineages that contributes to many different aspects of RNA metabolism during gene expression. Using photoactivated localization microscopy and single-molecule tracking, we demonstrate that Hfq forms a distinct and reversible focus-like structure in Escherichia coli specifically experiencing long-term nitrogen starvation. Using the ability of T7 phage to replicate in nitrogen-starved bacteria as a biological probe of E. coli cell function during nitrogen starvation, we demonstrate that Hfq foci have a role in the adaptive response of E. coli to long-term nitrogen starvation. We further show that Hfq foci formation does not depend on gene expression once nitrogen starvation has set in and occurs indepen-dently of the transcription factor N-regulatory protein C, which activates the initial adaptive response to N starvation in E. coli. These results serve as a paradigm to demonstrate that bacterial adaptation to long-term nutrient starvation can be spatiotemporally coordinated and can occur independently of de novo gene expression during starvation.

scholarly journals The Protease Lon and the RNA-Binding Protein Hfq Reduce Silencing of the Escherichia coli bgl Operon by H-NS

2004 ◽  
Vol 186 (9) ◽  
pp. 2708-2716 ◽  
Author(s):  
Sudhanshu Dole ◽  
Yvonne Klingen ◽  
V. Nagarajavel ◽  
Karin Schnetz
Keyword(s):  
Escherichia Coli ◽  
Transcription Initiation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Specific Effect ◽  
Receptor Protein ◽  
Coding Region ◽  
Genes Encoding ◽  
Pleiotropic Regulators

ABSTRACT The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon at two levels. H-NS binds upstream of the promoter, represses transcription initiation, and binds downstream within the coding region of the first gene, where it induces polarity of transcription elongation. In hns mutants, silencing of the bgl operon is completely relieved. Various screens for mutants in which silencing of bgl is reduced have yielded mutations in hns and in genes encoding the transcription factors LeuO and BglJ. In order to identify additional factors that regulate bgl, we performed a transposon mutagenesis screen for mutants in which silencing of the operon is strengthened. This screen yielded mutants with mutations in cyaA, hfq, lon, and pgi, encoding adenylate cyclase, RNA-binding protein Hfq, protease Lon, and phosphoglucose isomerase, respectively. In cyaA mutants, the cyclic AMP receptor protein-dependent promoter is presumably inactive. The specific effect of the pgi mutants on bgl is low. Interestingly, in the hfq and lon mutants, the downstream silencing of bgl by H-NS (i.e., the induction of polarity) is more efficient, while the silencing of the promoter by H-NS is unaffected. Furthermore, in an hns mutant, Hfq has no significant effect and the effect of Lon is reduced. These data provide evidence that the specific repression by H-NS can (directly or indirectly) be modulated and controlled by other pleiotropic regulators.

scholarly journals Small RNA ‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli

2020 ◽  
Vol 39 (6) ◽  
Author(s):  
Muna A Khan ◽  
Svetlana Durica‐Mitic ◽  
Yvonne Göpel ◽  
Ralf Heermann ◽  
Boris Görke
Keyword(s):  
Escherichia Coli ◽  
Small Rna ◽  
Rna Binding ◽  
Cell Envelope ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA-binding protein HF-I, known as a host factor for phage Qbeta RNA replication, is essential for rpoS translation in Escherichia coli.

1996 ◽  
Vol 10 (9) ◽  
pp. 1143-1151 ◽  
Author(s):  
A Muffler ◽  
D Fischer ◽  
R Hengge-Aronis
Keyword(s):  
Escherichia Coli ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Rna Replication ◽  
Host Factor
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