(Q38072253)

English

Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein

scientific article published on 05 January 2013

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scholarly article

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Europe PubMed Central

PubMed publication ID

28 August 2017

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Europe PubMed Central

Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 August 2017

author name string

Begoña Monterroso

1

1 reference

Europe PubMed Central

PubMed publication ID

28 August 2017

Carlos Alfonso

2

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Europe PubMed Central

PubMed publication ID

28 August 2017

Silvia Zorrilla

3

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Europe PubMed Central

PubMed publication ID

28 August 2017

Germán Rivas

4

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Europe PubMed Central

PubMed publication ID

28 August 2017

publication date

5 January 2013

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Europe PubMed Central

PubMed publication ID

28 August 2017

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Europe PubMed Central

PubMed publication ID

28 August 2017

59

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Europe PubMed Central

PubMed publication ID

28 August 2017

3

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Europe PubMed Central

PubMed publication ID

28 August 2017

349-362

1 reference

Europe PubMed Central

PubMed publication ID

28 August 2017

The order of the ring: assembly of Escherichia coli cell division components.

1 reference

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Bacterial cell division: assembly, maintenance and disassembly of the Z ring

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The cell as a collection of protein machines: preparing the next generation of molecular biologists

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Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

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Analytical ultracentrifugation for the study of protein association and assembly

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Strong FtsZ is with the force: mechanisms to constrict bacteria.

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FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.

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Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching

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Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins

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Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment

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The measurement of cooperative protein self-assembly by turbidity and other techniques

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Methods to measure actin polymerization

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Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function.

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Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain

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Reconstitution of contractile FtsZ rings in liposomes

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Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes.

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Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.

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Towards a bottom-up reconstitution of bacterial cell division.

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Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli

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Surface-Enhanced Raman scattering-based detection of the interactions between the essential cell division FtsZ protein and bacterial membrane elements.

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Biology under construction: in vitro reconstitution of cellular function.

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Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscs

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Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium

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On the analysis of sedimentation velocity in the study of protein complexes

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Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles

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Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium

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Analytical ultracentrifugation in a Gibbsian perspective

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Calcium-linked self-association of human complement C1s

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Ca(2+)-linked association of human complement C1s and C1r

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Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly

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Characterization of self-association and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering

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Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance

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Non-ideal tracer sedimentation equilibrium: a powerful tool for the characterization of macromolecular interactions in crowded solutions.

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Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: indefinite linear self-association of bacterial cell division protein FtsZ.

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Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution.

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Hemoglobin equilibrium analysis by the multiangle laser light-scattering method

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New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins

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Rapid quantitative characterization of protein interactions by composition gradient static light scattering.

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Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species

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10.1016/J.YMETH.2012.12.014

1 reference

Europe PubMed Central

PubMed publication ID

28 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 August 2017

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