The <scp>EAGR</scp> box structure: a motif involved in mycoplasma motility

Calisto, Bárbara M.; Broto, Alícia; Martinelli, Luca; Querol, Enrique; Piñol, Jaume; Fita, Ignacio

doi:10.1111/j.1365-2958.2012.08200.x

Cited by 17 publications

(27 citation statements)

References 40 publications

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“…MG200, the M. pneumoniae TopJ orthologous protein, was detected at wild‐type (WT) levels in Δmg491 cells. This protein has a specific role in gliding motility and might be involved in adhesin folding and translocation to the cell membrane (Pich et al ., ; Cloward and Krause, ; Calisto et al ., ). MG219 protein was also found at WT levels in Δmg491 cells indicating that deletion of MG_491 had no polar effects on the expression of the downstream MG_219 gene (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…Besides the interest as a human pathogen, this small flask-shaped bacterium with a genome of only 580 kb has attracted the attention of many researchers as a natural approach to a minimal cell (Glass et al, 2006;Karr et al, 2012). Unlike many mycoplasma species, methods for targeted gene deletion are available in M. genitalium (Dhandayuthapani et al, 1999;Burgos et al, 2006), making it possible to obtain well characterized mutant strains showing gliding deficiencies, loss of the adhesion properties and structural changes in the terminal organelle (Burgos et al, 2007Pich et al, 2008;Calisto et al, 2012; see also Table S1; Fig. S1).…”

Section: Introductionmentioning

confidence: 99%

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A minimized motile machinery for Mycoplasma genitalium

Garcia-Morales

González-González

Querol

et al. 2016

Molecular Microbiology

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SummaryThe cell wall-less bacterium Mycoplasma genitalium uses specialized adhesins located at the terminal organelle to adhere to host cells and surfaces. The terminal organelle is a polar structure protruding from the cell body that is internally supported by a cytoskeleton and also has an important role in cell motility. We have engineered a M. genitalium null mutant for MG491 protein showing a massive downstream destabilization of proteins involved in the terminal organelle organization. This mutant strain exhibited striking similarities with the previously isolated MG_218 null mutant strain. Upon introduction of an extra copy of MG_318 gene in both strains, the amount of main adhesins P140 and P110 dramatically increased. These strains were characterized by microcinematography, epifluorescence microscopy and cryo-electron microcopy, revealing the presence of motile cells and filaments in the absence of many proteins considered essential for cell adhesion and motility. These results indicate that adhesin complexes play a major role in the motile machinery of M. genitalium and demonstrate that the rod element of the cytoskeleton core is not the molecular motor propelling mycoplasma cells. These strains containing a minimized motile machinery also provide a valuable cell model to investigate the adhesion and gliding properties of this human pathogen.

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

A minimized motile machinery for Mycoplasma genitalium

Garcia-Morales

González-González

Querol

et al. 2016

Molecular Microbiology

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“…and Supporting Information Movie S4). P200 lacks homology to proteins of known function but has six ‘enriched in aromatic and glycine residues’ (EAGR) boxes, which were identified as protein interaction domains in the closely related Mycoplasma genitalium (Calisto et al ., ), and might mediate assembly into a higher‐order complex. Thus it came as a surprise here that loss of P200 did not visibly affect the major substructures at the base of the terminal organelle.…”

Section: Resultsmentioning

confidence: 99%

Electron cryotomography of Mycoplasma pneumoniae mutants correlates terminal organelle architectural features and function

Krause

Chen

Shi

et al. 2018

Molecular Microbiology

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The Mycoplasma pneumoniae terminal organelle functions in adherence and gliding motility and is comprised of at least eleven substructures. We used electron cryotomography to correlate impaired gliding and adherence function with changes in architecture in diverse terminal organelle mutants. All eleven substructures were accounted for in the prkC, prpC and P200 mutants, and variably so for the HMW3 mutant. Conversely, no terminal organelle substructures were evident in HMW1 and HMW2 mutants. The P41 mutant exhibits a terminal organelle detachment phenotype and lacked the bowl element normally present at the terminal organelle base. Complementation restored this substructure, establishing P41 as either a component of the bowl element or required for its assembly or stability, and that this bowl element is essential to anchor the terminal organelle but not for leverage in gliding. Mutants II-3, III-4 and topJ exhibited a visibly lower density of protein knobs on the terminal organelle surface. Mutants II-3 and III-4 lack accessory proteins required for a functional adhesin complex, while the topJ mutant lacks a DnaJ-like co-chaperone essential for its assembly. Taken together, these observations expand our understanding of the roles of certain terminal organelle proteins in the architecture and function of this complex structure.

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“…Further, two additional small GTPases act in concert with the bacteriofilin cytoskeleton to regulate the dynamic polarity properties of the cell upon which directional motility and reversal depend [Bulyha et al, 2013]. A dependency of cell shape and motility on the cytoskeleton is reminiscent of similar evidence for wall-less Mycoplasma and Spiroplasma cells [Calisto et al, 2012; Cohen-Krausz et al, 2011]. …”

Section: Poorly Characterized Types Of Bacterial Motilitymentioning

confidence: 99%

Microcompartments and Protein Machines in Prokaryotes

Saier

2013

Microb Physiol

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The prokaryotic cell was once thought of as a ‘bag of enzymes' with little or no intracellular compartmentalization. In this view, most reactions essential for life occurred as a consequence of random molecular collisions involving substrates, cofactors and cytoplasmic enzymes. Our current conception of a prokaryote is far from this view. We now consider a bacterium or an archaeon as a highly structured, nonrandom collection of functional membrane-embedded and proteinaceous molecular machines, each of which serves a specialized function. In this article we shall present an overview of such microcompartments including (1) the bacterial cytoskeleton and the apparati allowing DNA segregation during cell division; (2) energy transduction apparati involving light-driven proton pumping and ion gradient-driven ATP synthesis; (3) prokaryotic motility and taxis machines that mediate cell movements in response to gradients of chemicals and physical forces; (4) machines of protein folding, secretion and degradation; (5) metabolosomes carrying out specific chemical reactions; (6) 24-hour clocks allowing bacteria to coordinate their metabolic activities with the daily solar cycle, and (7) proteinaceous membrane compartmentalized structures such as sulfur granules and gas vacuoles. Membrane-bound prokaryotic organelles were considered in a recent Journal of Molecular Microbiology and Biotechnology written symposium concerned with membranous compartmentalization in bacteria [J Mol Microbiol Biotechnol 2013;23:1-192]. By contrast, in this symposium, we focus on proteinaceous microcompartments. These two symposia, taken together, provide the interested reader with an objective view of the remarkable complexity of what was once thought of as a simple noncompartmentalized cell.

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The EAGR box structure: a motif involved in mycoplasma motility

Cited by 17 publications

References 40 publications

A minimized motile machinery for Mycoplasma genitalium

A minimized motile machinery for Mycoplasma genitalium

Electron cryotomography of Mycoplasma pneumoniae mutants correlates terminal organelle architectural features and function

Microcompartments and Protein Machines in Prokaryotes

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