Active Transport of Membrane Components by Self-Organization of the Min Proteins

Shih, Yu‐Ling; Huang, Lingting; Tu, Yu-Ming; Lee, Bo-Fan; Bau, Yu-Chiuan; Hong, Chia Yee; Lee, Hsiao-Lin; Shih, Yan-Ping; Hsu, Min‐Feng; Chen, Jui-Szu; Lu, Zheng-Xin; Chao, Ling

doi:10.1101/418384

Cited by 2 publications

(3 citation statements)

References 27 publications

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“…5 ). The subsequent release from the membrane to bind again the mat S sites might be assisted by the oscillation behaviour of MinD that displaces proteins from the membrane surface of the new poles (32, 33). It is well known that the Min system oscillates between the old poles and the newly formed septum before the daughter cells have separated (34).…”

Section: Discussionmentioning

confidence: 99%

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

Monterroso¹,

Zorrilla²,

Sobrinos-Sanguino³

et al. 2018

Preprint

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word count: 329 26 Text word count: 5924 27 28 29 30 2ABSTRACT Division ring formation at midcell is controlled by various mechanisms in 31 Escherichia coli, one of them being the linkage between the chromosomal Ter macrodomain and 32 the Z-ring mediated by MatP, a DNA binding protein that organizes this macrodomain and 33 contributes to the prevention of premature chromosome segregation. Here we show that, during 34 cell division, just before splitting the daughter cells, MatP seems to localize close to the 35 cytoplasmic membrane, suggesting that this protein might interact with lipids. To test this 36 hypothesis, we investigated MatP interaction with lipids in vitro. We found that MatP, when 37 encapsulated inside microdroplets generated by microfluidics and giant vesicles, accumulates at 38 phospholipid bilayers and monolayers matching the lipid composition in the E. coli inner 39 membrane. MatP binding to lipids was independently confirmed using lipid coated microbeads 40 and bio-layer interferometry assays. Interaction of MatP with the lipid membranes also occurs in 41 the presence of the DNA sequences specifically targeted by the protein but there is no evidence 42 of ternary membrane/protein/DNA complexes. We propose that the interaction of MatP with 43 lipids may modulate its spatiotemporal localization and its recognition of other ligands. 44 IMPORTANCE The division of an E. coli cell into two daughter cells with equal genomic 45 information and similar size requires duplication and segregation of the chromosome and 46 subsequent scission of the envelope by a protein ring, the Z-ring. MatP is a DNA binding protein 47 51 MatP. This observation strongly suggests that the membrane may play a role in the regulation of 52 the function and localization of MatP, which could be relevant for the coordination of the two 53 fundamental processes in which this protein participates, nucleoid segregation and cell division. 54 55 56 KEYWORDS bacterial division, DNA binding proteins, protein-membrane interaction, division 57 site selection, biochemical reconstruction 58 59 60 61

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Section: Discussionmentioning

confidence: 99%

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

Monterroso¹,

Zorrilla²,

Sobrinos-Sanguino³

et al. 2018

Preprint

View full text Add to dashboard Cite

show abstract

Section: Figurementioning

confidence: 99%

“…While there is a significant body of knowledge on how lipid composition and dynamics affect membrane-bound enzymes, 5,6 little is known, regarding the effect of enzyme catalysis on the motility and lateral transport in lipid bilayers in cells. 7 Due to the high complexity and heterogeneity of cell membranes, it is difficult to identify the specific mechanisms for lateral mobility and spatial reorganization in live cell membranes.…”

mentioning

confidence: 99%

Enzyme Catalysis Enhances Lateral Lipid Motility and Directional Particle Transport on Membranes

Somasundar

Mandal

Sen

2021

Preprint

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The dynamic interplay between the composition of lipid membranes and the behavior of membrane-bound enzymes is critical to the understanding of cellular function and viability, and the design of membrane-based biosensing platforms. While there is a significant body of knowledge on how lipid composition and dynamics affect membrane-bound enzymes, little is known about how enzyme catalysis influences the motility and lateral transport in lipid membranes. Using enzymes-attached lipids in supported bilayers (SLB), we show catalysis-induced enhanced lateral diffusion of lipids in the bilayer. Enhancing the membrane viscosity by increasing the cholesterol content in the bilayer suppresses the overall diffusion but not the relative diffusion enhancement of the enzyme-attached lipids. We also provide direct evidence of catalysis-induced membrane fluctuations leading to the enhanced diffusion of passive tracers resting on the SLB. Additionally, by using active enzyme patches, we demonstrate the directional transport of tracers on SLBs. These are first steps in understanding diffusion and transport in lipid membranes due to active, out-of-equilibrium processes that are the hallmark of living systems. In general, our study demonstrates how active enzymes can be used to control diffusion and transport in confined 2-D environments.

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Active Transport of Membrane Components by Self-Organization of the Min Proteins

Cited by 2 publications

References 27 publications

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

Enzyme Catalysis Enhances Lateral Lipid Motility and Directional Particle Transport on Membranes

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