Role of the sfiA-dependent cell division regulation system in Escherichia coli.

One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information has been collected to understand the functional mechanism of these pumps, especially with AcrAB-TolC from Escherichia coli, but one missing piece from all the suggested models is the role of peptidoglycan in the assembly. Here, by pull-down experiments with purified peptidoglycans, we precise the MexAB-OprM interaction with the peptidoglycan from Escherichia coli and Pseudomonas aeruginosa, highlighting a role of the peptidoglycan in stabilizing the MexA-OprM complex and also differences between the two Gram-negative bacteria peptidoglycans.

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The Tat system and its dependent cell division proteins are critical for virulence of extra-intestinal pathogenic Escherichia coli

Virulence ◽

10.1080/21505594.2020.1817709 ◽

2020 ◽

Vol 11 (1) ◽

pp. 1279-1292

Author(s):

Jinjin Liu ◽

Fan Yin ◽

Te Liu ◽

Shaowen Li ◽

Chen Tan ◽

...

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Pathogenic Escherichia Coli ◽

Dependent Cell ◽

Tat System

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Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site

Journal of Bacteriology ◽

10.1128/jb.00723-07 ◽

2007 ◽

Vol 189 (20) ◽

pp. 7273-7280 ◽

Cited By ~ 16

Author(s):

Dirk-Jan Scheffers ◽

Carine Robichon ◽

Gert Jan Haan ◽

Tanneke den Blaauwen ◽

Gregory Koningstein ◽

...

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Membrane Protein ◽

Cytoplasmic Membrane ◽

Central Component ◽

Transmembrane Segment ◽

Division Site ◽

Periplasmic Domain ◽

Cell Division Protein

ABSTRACT The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the role of the transmembrane segment (TMS) that anchors FtsQ in the cytoplasmic membrane. A set of TMS mutants was made and analyzed for the ability to complement an ftsQ mutant. Study of the various steps involved in FtsQ biogenesis revealed that one mutant (L29/32R;V38P) failed to functionally insert into the membrane, whereas another mutant (L29/32R) was correctly assembled and interacted with FtsB and FtsL but failed to localize efficiently to the cell division site. Our results indicate that the FtsQ TMS plays a role in FtsQ localization to the division site.

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The Role of the Arabidopsis E2FB Transcription Factor in Regulating Auxin-Dependent Cell Division

The Plant Cell ◽

10.1105/tpc.105.033761 ◽

2005 ◽

Vol 17 (9) ◽

pp. 2527-2541 ◽

Cited By ~ 119

Author(s):

Zoltán Magyar ◽

Lieven De Veylder ◽

Ana Atanassova ◽

László Bakó ◽

Dirk Inzé ◽

...

Keyword(s):

Transcription Factor ◽

Cell Division ◽

Dependent Cell

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TusA is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli

Journal of Bacteriology ◽

10.1128/jb.00659-20 ◽

2021 ◽

Author(s):

Tugba Yildiz ◽

Silke Leimkühler

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Major Effect ◽

Translational Efficiency ◽

Translation Efficiency ◽

Sulfur Transfer ◽

Wobble Position ◽

Filamentous Cell ◽

Sulfur Trafficking

To enable accurate and efficient translation, sulfur modifications are introduced posttranscriptionally into nucleosides in tRNAs. The biosynthesis of tRNA sulfur modifications involves unique sulfur trafficking systems for the incorporation of sulfur atoms in different nucleosides of tRNA. One of the proteins that is involved in inserting the sulfur for 5-methylaminomethyl-2-thiouridine (mnm5s2U34) modifications in tRNAs is the TusA protein. TusA, however, is a versatile protein that is also involved in numerous other cellular pathways. Despite its role as a sulfur transfer protein for the 2-thiouridine formation in tRNA, a fundamental role of TusA in the general physiology of Escherichia coli has also been discovered. Poor viability, a defect in cell division, and a filamentous cell morphology have been described previously for tusA-deficient cells. In this report, we aimed to dissect the role of TusA for cell viability. We were able to show that the lack of the thiolation status of wobble uridine (U34) nucleotides present on Lys, Gln, or Glu in tRNAs has a major consequence on the translation efficiency of proteins; among the affected targets are the proteins RpoS and Fis. Both proteins are major regulatory factors, and the deregulation of their abundance consequently has a major effect on the cellular regulatory network, with one consequence being a defect in cell division by regulating the FtsZ ring formation. IMPORTANCE More than 100 different modifications are found in RNAs. One of these modifications is the mnm5s2U modification at the wobble position 34 of tRNAs for Lys, Gln, and Glu. The functional significance of U34 modifications is substantial since it restricts the conformational flexibility of the anticodon, thus providing translational fidelity. We show that in an Escherichia coli TusA mutant strain, involved in sulfur transfer for the mnm5s2U34 thio modifications, the translation efficiency of RpoS and Fis, two major cellular regulatory proteins, is altered. Therefore, in addition to the transcriptional regulation and the factors that influence protein stability, tRNA modifications that ensure the translational efficiency provide an additional crucial regulatory factor for protein synthesis.

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Role of rec genes in SOS-induced inhibition of cell division in Escherichia coli

Mutation Research Letters ◽

10.1016/0165-7992(87)90064-9 ◽

1987 ◽

Vol 192 (4) ◽

pp. 247-252 ◽

Cited By ~ 6

Author(s):

Jelena Knežević-Vukčević ◽

Branka Vuković ◽

Draga Simić

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Rec Genes

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Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring

Molecular Microbiology ◽

10.1111/j.1365-2958.2010.07134.x ◽

2010 ◽

Vol 76 (3) ◽

pp. 760-771 ◽

Cited By ~ 44

Author(s):

Ana Isabel Rico ◽

Marta García-Ovalle ◽

Pilar Palacios ◽

Mercedes Casanova ◽

Miguel Vicente

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Division Ring

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Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

Journal of Bacteriology ◽

10.1128/jb.182.22.6366-6373.2000 ◽

2000 ◽

Vol 182 (22) ◽

pp. 6366-6373 ◽

Cited By ~ 51

Author(s):

Lucía Yim ◽

Guy Vandenbussche ◽

Jesús Mingorance ◽

Sonsoles Rueda ◽

Mercedes Casanova ◽

...

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Biological Function ◽

Wild Type ◽

Carboxy Terminus ◽

Yeast Two Hybrid ◽

Yeast Two Hybrid System ◽

Carboxy Terminal ◽

Two Hybrid

ABSTRACT The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of theftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutation (Gayda et al., J. Bacteriol. 174:5362–5370, 1992), suggesting that an interaction of FtsA with itself might play a role in its function. The existence of such an interaction was demonstrated using the yeast two-hybrid system and a protein overlay assay. Even these short deletions are sufficient for impairing the interaction of the truncated FtsA forms with the wild-type protein in the yeast two-hybrid system. The existence of additional interactions between FtsA molecules, involving other domains, can be postulated from the interaction properties shown by the FtsA deletion mutant forms, because although unable to interact with the wild-type and with FtsAΔ1, they can interact with themselves and cross-interact with each other. The secondary structures of an extensive deletion, FtsAΔ27, and the wild-type protein are indistinguishable when analyzed by Fourier transform infrared spectroscopy, and moreover, FtsAΔ27 retains the ability to bind ATP. These results indicate that deletion of the carboxy-terminal 27 residues does not alter substantially the structure of the protein and suggest that the loss of biological function of the carboxy-terminal deletion mutants might be related to the modification of their interacting properties.

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SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli

mBio ◽

10.1128/mbio.02796-20 ◽

2020 ◽

Vol 11 (6) ◽

Author(s):

Manuel Pazos ◽

Katharina Peters ◽

Adrien Boes ◽

Yalda Safaei ◽

Calem Kenward ◽

...

Keyword(s):

Escherichia Coli ◽

Cell Division ◽

Binding Proteins ◽

Cell Envelope ◽

Synthetic Activity ◽

Penicillin Binding Protein ◽

Direct Role ◽

Content Type ◽

Class A

ABSTRACT Sporulation-related repeat (SPOR) domains are present in many bacterial cell envelope proteins and are known to bind peptidoglycan. Escherichia coli contains four SPOR proteins, DamX, DedD, FtsN, and RlpA, of which FtsN is essential for septal peptidoglycan synthesis. DamX and DedD may also play a role in cell division, based on mild cell division defects observed in strains lacking these SPOR domain proteins. Here, we show by nuclear magnetic resonance (NMR) spectroscopy that the periplasmic part of DedD consists of a disordered region followed by a canonical SPOR domain with a structure similar to that of the SPOR domains of FtsN, DamX, and RlpA. The absence of DamX or DedD decreases the functionality of the bifunctional transglycosylase-transpeptidase penicillin-binding protein 1B (PBP1B). DamX and DedD interact with PBP1B and stimulate its glycosyltransferase activity, and DamX also stimulates the transpeptidase activity. DedD also binds to PBP1A and stimulates its glycosyltransferase activity. Our data support a direct role of DamX and DedD in enhancing the activity of PBP1B and PBP1A, presumably during the synthesis of the cell division septum. IMPORTANCE Escherichia coli has four SPOR proteins that bind peptidoglycan, of which FtsN is essential for cell division. DamX and DedD are suggested to have semiredundant functions in cell division based on genetic evidence. Here, we solved the structure of the SPOR domain of DedD, and we show that both DamX and DedD interact with and stimulate the synthetic activity of the peptidoglycan synthases PBP1A and PBP1B, suggesting that these class A PBP enzymes act in concert with peptidoglycan-binding proteins during cell division.

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