Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein

Hj, Defeu Soufo; Reimold, Christian; Linne, Uwe; Knust, T; Gescher, Johannes; Graumann, Peter L.

doi:10.1073/pnas.0911979107

Cited by 101 publications

(65 citation statements)

References 42 publications

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“…18c). This is in striking contrast with the situation that when only MreB or MreB-mEosC was overexpressed, the bacterial cells tended to grow longer, consistent with previously reported observation29.…”

Section: Resultssupporting

confidence: 91%

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Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space

Liu

Xing

et al. 2014

Nat Commun

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Imaging the location and dynamics of individual interacting protein pairs is essential but often difficult because of the fluorescent background from other paired and non-paired molecules, particularly in the sub-diffraction cellular space. Here we develop a new method combining bimolecular fluorescence complementation and photoactivated localization microscopy for super-resolution imaging and single-molecule tracking of specific protein–protein interactions. The method is used to study the interaction of two abundant proteins, MreB and EF-Tu, in Escherichia coli cells. The super-resolution imaging shows interesting distribution and domain sizes of interacting MreB–EF-Tu pairs as a subpopulation of total EF-Tu. The single-molecule tracking of MreB, EF-Tu and MreB–EF-Tu pairs reveals intriguing localization-dependent heterogonous dynamics and provides valuable insights to understanding the roles of MreB–EF-Tu interactions.

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Section: Resultssupporting

confidence: 91%

“…9a) might be again due to the perturbance from Snap-tag in mEosN-EFTu-Snap or the stress induced by electroporation. Unlike the high level of overlapping observed by conventional fluorescence imaging29, co-localization between EF-Tu and MreB seemed rather low in the super-resolution images (Supplementary Fig. 10b).…”

Section: Resultsmentioning

confidence: 66%

Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space

Liu

Xing

et al. 2014

Nat Commun

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“…Specifically, to affect the longitudinal stiffness of cells, MreB would need to remain attached to the cell membrane for a time scale that is incompatible with the rapid turnover of MreB filaments, their detachment from the cell wall, their diffusion, and their reattachment to the cell wall to coordinate peptidoglycan growth. 109 …”

Section: Bacterial Proteins That Hypothetically Contribute To Cell Stmentioning

confidence: 99%

Bacterial Cell Mechanics

2017

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Cellular mechanical properties play an integral role in bacterial survival and adaptation. Historically, the bacterial cell wall and, in particular, the layer of polymeric material called the peptidoglycan were the elements to which cell mechanics could be primarily attributed. Disrupting the biochemical machinery that assembles the peptidoglycan (e.g., using the β-lactam family of antibiotics) alters the structure of this material, leads to mechanical defects, and results in cell lysis. Decades after the discovery of peptidoglycan-synthesizing enzymes, the mechanisms that underlie their positioning and regulation are still not entirely understood. In addition, recent evidence suggests a diverse group of other biochemical elements influence bacterial cell mechanics, may be regulated by new cellular mechanisms, and may be triggered in different environmental contexts to enable cell adaptation and survival. This review summarizes the contributions that different biomolecular components of the cell wall (e.g., lipopolysaccharides, wall and lipoteichoic acids, lipid bilayers, peptidoglycan, and proteins) make to Gram-negative and Gram-positive bacterial cell mechanics. We discuss the contribution of individual proteins and macromolecular complexes in cell mechanics and the tools that make it possible to quantitatively decipher the biochemical machinery that contributes to bacterial cell mechanics. Advances in this area may provide insight into new biology and influence the development of antibacterial chemotherapies.

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“…The decreased secretion of SipD, a T3SS-1 invasion protein, in the AMPR mutants may alter the ability of these cells to invade host tissue (20). Mutations in AMPR genes also caused an increase in the levels of proteins in the supernatant that are naturally found in the cell membrane (Tuf [59]), in the periplasm (OsmY, MalE, and GlpQ [60][61][62]), or in the cytosol (Tsf and GapA [63,64]). The decreased secretion of flagellar proteins and the increased presence of membrane proteins in the supernatants of the ⌬virK ⌬ybjX mutant and the ⌬ybjX mutant indicate an unstable outer membrane or membrane shearing.…”

Section: Fig 10mentioning

confidence: 99%

Salmonella enterica Serovar Enteritidis Antimicrobial Peptide Resistance Genes Aid in Defense against Chicken Innate Immunity, Fecal Shedding, and Egg Deposition

et al. 2014

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c Salmonella enterica serovar Enteritidis (S. Enteritidis) is a major etiologic agent of nontyphoid salmonellosis in the United States. S. Enteritidis persistently and silently colonizes the intestinal and reproductive tract of laying hens, resulting in contaminated poultry products. The consumption of contaminated poultry products has been identified as a significant risk factor for human salmonellosis. To understand the mechanisms S. Enteritidis utilizes to colonize and persist in laying hens, we used selective capture of transcribed sequences to identify genes overexpressed in the HD11 chicken macrophage cell line and in primary chicken oviduct epithelial cells. From the 15 genes found to be overexpressed in both cell types, we characterized the antimicrobial peptide resistance (AMPR) genes, virK and ybjX, in vitro and in vivo. In vitro, AMPR genes were required for natural morphology, motility, secretion, defense against detergents such as EDTA and bile salts, and resistance to antimicrobial peptides polymyxin B and avian ␤-defensins. From this, we inferred the AMPR genes play a role in outer membrane stability and/or modulation. In the intestinal tract, AMPR genes were involved in early intestinal colonization and fecal shedding. In the reproductive tract, virK was required in early colonization whereas a deletion of ybjX caused prolonged ovary colonization and egg deposition. Data from the present study indicate that AMPR genes are differentially utilized in various host environments, which may ultimately assist S. Enteritidis in persistent and silent colonization of chickens.

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Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein

Cited by 101 publications

References 42 publications

Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space

Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space

Bacterial Cell Mechanics

Salmonella enterica Serovar Enteritidis Antimicrobial Peptide Resistance Genes Aid in Defense against Chicken Innate Immunity, Fecal Shedding, and Egg Deposition

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