scholarly journals Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis

2022 ◽  
Author(s):  
Ben F Luisi ◽  
Md. Saiful Islam ◽  
Steven William Hardwick ◽  
Laura Quell ◽  
Dimitri Y Chirgadze ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacterial Cell ◽  
Quaternary Structure ◽  
Cell Envelope ◽  
Evolutionary Relationship ◽  
Regulatory Rna ◽  
Rnase E ◽  
Small Regulatory Rna ◽  
Conserved Domain ◽  
Transcription Networks

The biogenesis of the essential precursor of the bacterial cell envelope, glucosamine-6-phosphate (GlcN6P), is controlled through intricate post-transcription networks mediated by GlmZ, a small regulatory RNA (sRNA). GlmZ stimulates translation of the mRNA encoding GlcN6P synthetase in Escherichia coli, but when bound by the protein RapZ, it becomes inactivated through cleavage by the endoribonuclease RNase E. Here we report the cryoEM structure of the RapZ:GlmZ complex, revealing a complementary match of the protein tetrameric quaternary structure to an imperfect structural repeat in the RNA. The RNA is contacted mostly through a highly conserved domain of RapZ that shares deep evolutionary relationship with phosphofructokinase and suggests links between metabolism and riboregulation. We also present the structure of a pre-cleavage encounter intermediate formed between the binary RapZ:GlmZ complex and RNase E that reveals how GlmZ is presented and recognised for cleavage. The structures suggest how other encounter complexes might guide recognition and action of endoribonucleases on target transcripts, and how structured substrates in polycistronic precursors are recognised for processing.

scholarly journals Targeting of csgD by the small regulatory RNA RprA links stationary phase, biofilm formation and cell envelope stress in Escherichia coli

2012 ◽  
Vol 84 (1) ◽  
pp. 51-65 ◽  
Author(s):  
Franziska Mika ◽  
Susan Busse ◽  
Alexandra Possling ◽  
Janine Berkholz ◽  
Natalia Tschowri ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Biofilm Formation ◽  
Cell Envelope ◽  
Regulatory Rna ◽  
Small Regulatory Rna ◽  
Envelope Stress

Mo1770 Expression of the Oxys Small Regulatory RNA in Luminal Commensal Escherichia coli Attenuates Experimental Colitis

2012 ◽  
Vol 142 (5) ◽  
pp. S-681
Author(s):  
Sandrine Y. Tchaptchet ◽  
Ting-Jia Fan ◽  
Laura E. Goeser ◽  
Ryan B. Sartor ◽  
Jonathan J. Hansen
Keyword(s):  
Escherichia Coli ◽  
Experimental Colitis ◽  
Regulatory Rna ◽  
Small Regulatory Rna

scholarly journals Kinetics and mechanism of the bactericidal action of human neutrophils against Escherichia coli

Blood ◽  
1984 ◽  
Vol 64 (3) ◽  
pp. 635-641
Author(s):  
MN Hamers ◽  
AA Bot ◽  
RS Weening ◽  
HJ Sips ◽  
D Roos
Keyword(s):  
Escherichia Coli ◽  
Computer Program ◽  
Rate Constants ◽  
Bacterial Cell ◽  
Cell Envelope ◽  
Human Neutrophils ◽  
Galactosidase Activity ◽  
E Coli ◽  
Bacterial Proteins ◽  
Beta Galactosidase

A mutant strain of Escherichia coli (E. coli ML-35) was used to follow the kinetics of phagocytosis, perforation of the bacterial cell envelope, and inactivation of bacterial proteins by human neutrophils. This particular E. coli mutant strain has no lactose permease, but constitutively forms the cytoplasmic enzyme beta-galactosidase. This implies that the artificial substrate ortho-nitrophenyl-beta-D- galactopyranoside cannot reach the beta-galactosidase unless the bacterial cell envelope has been perforated. Thus, the integrity of the E. coli envelope can be measured simply by the activity of beta- galactosidase with this substrate. Indeed, ingestion of E. coli ML-35 by human neutrophils was followed by perforation of the bacteria (increase in beta-galactosidase activity). Subsequently, the beta- galactosidase activity decreased due to inactivation of the enzyme. With a simple mathematical model and a curve-fitting computer program, we have determined the first-order rate constants for phagocytosis, perforation, and beta-galactosidase inactivation. With 32 normal donors, we found an interdonor variation in these rate constants of 20% to 30% (SD) and an assay variance of 5%. The perforation process closely correlated with the loss of colony-forming capacity of the bacteria. This new assay measures phagocytosis and killing in a fast, simple, and accurate way; it is not hindered by extracellular bacteria. Moreover, this method also measures the postkilling event of inactivation of a bacterial protein, which permits a better detection of neutrophils deficient in this function. The assay can also be used for screening neutrophil functions without the use of a computer program. A simple calculation suffices to detect neutrophil abnormalities. Neutrophils from patients with chronic granulomatous disease (CGD) showed an impaired rate of perforation and thus also of inactivation. Neutrophils from myeloperoxidase-deficient patients or from a patient with the Chediak-Higashi syndrome only showed a retarded inactivation of beta-galactosidase, but normal ingestion and perforation. The role of myeloperoxidase in the killing process is discussed. Although myeloperoxidase does not seem to be a prerequisite for perforation, it probably plays a role in bacterial destruction by normal cells, because the inactivation of bacterial proteins seems strictly myeloperoxidase dependent.

A novel small regulatory RNA enhances cell motility in enterohemorrhagic Escherichia coli

2014 ◽  
Vol 60 (1) ◽  
pp. 44-50 ◽  
Author(s):  
Naoki Sudo ◽  
Akiko Soma ◽  
Akira Muto ◽  
Sunao Iyoda ◽  
Mayumi Suh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Motility ◽  
Enterohemorrhagic Escherichia Coli ◽  
Regulatory Rna ◽  
Small Regulatory Rna

scholarly journals Adaptor protein RapZ activates endoribonuclease RNase E by protein–protein interaction to cleave a small regulatory RNA

RNA ◽  
2020 ◽  
Vol 26 (9) ◽  
pp. 1198-1215
Author(s):  
Svetlana Durica-Mitic ◽  
Yvonne Göpel ◽  
Fabian Amman ◽  
Boris Görke
Keyword(s):  
Protein Interaction ◽  
Adaptor Protein ◽  
Regulatory Rna ◽  
Rnase E ◽  
Protein Protein Interaction ◽  
Small Regulatory Rna

scholarly journals Kinetics and mechanism of the bactericidal action of human neutrophils against Escherichia coli

Blood ◽  
1984 ◽  
Vol 64 (3) ◽  
pp. 635-641 ◽  
Author(s):  
MN Hamers ◽  
AA Bot ◽  
RS Weening ◽  
HJ Sips ◽  
D Roos
Keyword(s):  
Escherichia Coli ◽  
Computer Program ◽  
Rate Constants ◽  
Bacterial Cell ◽  
Cell Envelope ◽  
Human Neutrophils ◽  
Galactosidase Activity ◽  
E Coli ◽  
Bacterial Proteins ◽  
Beta Galactosidase

Abstract A mutant strain of Escherichia coli (E. coli ML-35) was used to follow the kinetics of phagocytosis, perforation of the bacterial cell envelope, and inactivation of bacterial proteins by human neutrophils. This particular E. coli mutant strain has no lactose permease, but constitutively forms the cytoplasmic enzyme beta-galactosidase. This implies that the artificial substrate ortho-nitrophenyl-beta-D- galactopyranoside cannot reach the beta-galactosidase unless the bacterial cell envelope has been perforated. Thus, the integrity of the E. coli envelope can be measured simply by the activity of beta- galactosidase with this substrate. Indeed, ingestion of E. coli ML-35 by human neutrophils was followed by perforation of the bacteria (increase in beta-galactosidase activity). Subsequently, the beta- galactosidase activity decreased due to inactivation of the enzyme. With a simple mathematical model and a curve-fitting computer program, we have determined the first-order rate constants for phagocytosis, perforation, and beta-galactosidase inactivation. With 32 normal donors, we found an interdonor variation in these rate constants of 20% to 30% (SD) and an assay variance of 5%. The perforation process closely correlated with the loss of colony-forming capacity of the bacteria. This new assay measures phagocytosis and killing in a fast, simple, and accurate way; it is not hindered by extracellular bacteria. Moreover, this method also measures the postkilling event of inactivation of a bacterial protein, which permits a better detection of neutrophils deficient in this function. The assay can also be used for screening neutrophil functions without the use of a computer program. A simple calculation suffices to detect neutrophil abnormalities. Neutrophils from patients with chronic granulomatous disease (CGD) showed an impaired rate of perforation and thus also of inactivation. Neutrophils from myeloperoxidase-deficient patients or from a patient with the Chediak-Higashi syndrome only showed a retarded inactivation of beta-galactosidase, but normal ingestion and perforation. The role of myeloperoxidase in the killing process is discussed. Although myeloperoxidase does not seem to be a prerequisite for perforation, it probably plays a role in bacterial destruction by normal cells, because the inactivation of bacterial proteins seems strictly myeloperoxidase dependent.

The Escherichia Coli Small Regulatory Rna Oxys Impairs Bacterial Translocation and Attenuates Experimental Colitis

2017 ◽  
Vol 152 (5) ◽  
pp. S1000
Author(s):  
Diana Arsene ◽  
Sandrine Y. Tchaptchet ◽  
Ting-Jia Fan ◽  
Jonathan J. Hansen
Keyword(s):  
Escherichia Coli ◽  
Bacterial Translocation ◽  
Experimental Colitis ◽  
Regulatory Rna ◽  
Small Regulatory Rna
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