Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding

Mazor, Shirley; Regev, Tomer; Mileykovskaya, Eugenia; Margolin, William; Dowhan, William; Fishov, Itzhak

doi:10.1016/j.bbamem.2008.08.004

Cited by 21 publications

(14 citation statements)

References 40 publications

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“…We propose that the mechanical stress in the membrane structure caused by binding of the initiation or dissociation centers affects the affinity of the membrane in the neighborhood of the complex to additional protein binding. Distortion of the membrane structure by MinD binding has been evidenced by the previous observation that unilamellar vesicles are converted to thin tubes by high-density binding of MinD (32), as well as recent fluorescence anisotropy and calorimetry studies of MinD interactions with lipid membranes (37,38). The above "membrane stress" hypothesis also explains additional aspects of our results as discussed below.…”

Section: Discussionsupporting

confidence: 64%

Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins

Ivanov

Mizuuchi

2010

Proc. Natl. Acad. Sci. U.S.A.

112

150

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Min proteins of the Escherichia coli cell division system oscillate between the cell poles in vivo. In vitro on a solid-surface supported lipid bilayer, these proteins exhibit a number of interconverting modes of collective ATP-driven dynamic pattern formation including not only the previously described propagating waves, but also near uniformity in space surface concentration oscillation, propagating filament like structures with a leading head and decaying tail and moving and dividing amoeba-like structures with sharp edges. We demonstrate that the last behavior most closely resembles in vivo system behavior. The simple reaction-diffusion models previously proposed for the Min system fail to explain the results of the in vitro self-organization experiments. We propose the hypotheses that initiation of MinD binding to the surface is controlled by counteraction of initiation and dissociation complexes; the binding of MinD/E is stimulated by MinE and involves polymerization-depolymerization dynamics; polymerization of MinE over MinD oligomers triggers dynamic instability leading to detachment from the membrane. The physical properties of the lipid bilayer are likely to be one of the critical determinants of certain aspects of the dynamic patterns observed.cell division | min system | oscillations and waves | self-organization | septum localization

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Section: Discussionsupporting

confidence: 64%

Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins

Ivanov

Mizuuchi

2010

Proc. Natl. Acad. Sci. U.S.A.

112

150

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“…Possibly, the membrane potential results in a subtle conformational change of the amphipathic helix that enhances binding. On the other hand, it has been shown that binding of MinD is stimulated when the membrane fluidity is increased (27). Interestingly, membrane fluidity can also be increased by imposing a ΔΨ (28).…”

Section: Resultsmentioning

confidence: 98%

Membrane potential is important for bacterial cell division

Strahl

Hamoen

2010

Proc. Natl. Acad. Sci. U.S.A.

462

463

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Many cell division-related proteins are located at specific positions in the bacterial cell, and this organized distribution of proteins requires energy. Here, we report that the proton motive force, or more specifically the (trans)membrane potential, is directly involved in protein localization. It emerged that the membrane potential modulates the distribution of several conserved cell division proteins such as MinD, FtsA, and the bacterial cytoskeletal protein MreB. We show for MinD that this is based on the membrane potential stimulated binding of its C-terminal amphipathic helix. This function of the membrane potential has implications for how these morphogenetic proteins work and provide an explanation for the effects observed with certain antimicrobial compounds.

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“…The co-localization of MadR1-GFP foci and FM 4–64 Fx hotspots indicates a connection between MadR1 activity and anionic phospholipid domains. MadR1 may localize to pre-established domains for activation as has been observed for several other membrane-associated proteins, or may stimulate the production of acidic phospholipids [31–32]. It is possible these co-localized hotspots are due to the formation of lipid bodies resulting from protein overproduction or GFP fusion, however certain behaviors are unlikely to be attributed to lipid bodies.…”

Section: Discussionmentioning

confidence: 99%

MadR1, a Mycobacterium tuberculosis cell cycle stress response protein that is a member of a widely conserved protein class of prokaryotic, eukaryotic and archeal origin

et al. 2015

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SUMMARY Stress-induced molecular programs designed to stall division progression are nearly ubiquitous in bacteria, with one well-known example being the participation of the SulA septum inhibiting protein in the SOS DNA damage repair response. Mycobacteria similarly demonstrate stress-altered growth kinetics, however no such regulators have been found in these organisms. We therefore set out to identify SulA-like regulatory proteins in Mycobacterium tuberculosis. A bioinformatics modeling-based approach led to the identification of rv2216 as encoding for a protein with weak similarity to SulA, further analysis distinguished this protein as belonging to a group of previously uncharacterized growth promoting proteins. We have named the mycobacterial protein encoded by rv2216 morphology altering division regulator protein 1, MadR1. Overexpression of madR1 modulated cell length while maintaining growth kinetics similar to wild-type, and increased the proportion of bent or V-form cells in the population. The presence of MadR1-GFP at regions of cellular elongation (poles) and morphological differentiation (V-form) suggests MadR1 involvement in phenotypic herterogeneity and longitudinal cellular growth. Global transcriptional analysis indicated that MadR1 functionality is linked to lipid editing programs required for growth and persistence. This is the first report to differentiate the larger class of these conserved proteins from SulA proteins and characterizes MadR1 effects on the mycobacterial cell.

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Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding

Cited by 21 publications

References 40 publications

Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins

Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins

Membrane potential is important for bacterial cell division

MadR1, a Mycobacterium tuberculosis cell cycle stress response protein that is a member of a widely conserved protein class of prokaryotic, eukaryotic and archeal origin

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