Early targeting of Min proteins to the cell poles in germinated spores of Bacillus subtilis: evidence for division apparatus-independent recruitment of Min proteins to the division site

2008 ◽  
Vol 47 (1) ◽  
pp. 37-48 ◽  
Author(s):  
Elizabeth J. Harry ◽  
Peter J. Lewis
Keyword(s):  
Bacillus Subtilis ◽  
Division Site ◽  
Min Proteins

scholarly journals Dynamics of the Bacillus subtilis Min system

2020 ◽  
Author(s):  
Helge Feddersen ◽  
Laeschkir Würthner ◽  
Erwin Frey ◽  
Marc Bramkamp
Keyword(s):  
Bacillus Subtilis ◽  
Active Sites ◽  
Dynamic Equilibrium ◽  
Model Organism ◽  
Physical Modelling ◽  
Division Site ◽  
Diffusion Constants ◽  
Dynamic Equilibrium State ◽  
Min Proteins

SummaryDivision site selection is a vital process to ensure generation of viable offspring. In many rod-shaped bacteria a dynamic protein system, termed the Min system, acts as a central regulator of division site placement. The Min system is best studied in Escherichia coli where it shows a remarkable oscillation from pole to pole with a time-averaged density minimum at midcell. Several components of the Min system are conserved in the Gram-positive model organism Bacillus subtilis. However, in B. subtilis it is believed that the system forms a stationary bipolar gradient from the cell poles to midcell. Here, we show that the Min system of B. subtilis localizes dynamically to active sites of division, often organized in clusters. We provide physical modelling using measured diffusion constants that describe the observed enrichment of the Min system at the septum. Modelling suggests that the observed localization pattern of Min proteins corresponds to a dynamic equilibrium state. Our data provide evidence for the importance of ongoing septation for the Min dynamics, consistent with a major role of the Min system to control active division sites, but not cell pole areas.

scholarly journals Dynamics of the Bacillus subtilis Min System

mBio ◽  
2021 ◽  
Vol 12 (2) ◽  
Author(s):  
Helge Feddersen ◽  
Laeschkir Würthner ◽  
Erwin Frey ◽  
Marc Bramkamp
Keyword(s):  
Bacillus Subtilis ◽  
Protein Dynamics ◽  
Site Selection ◽  
Active Sites ◽  
Molecular Mechanisms ◽  
Content Type ◽  
E Coli ◽  
Protein System ◽  
Division Site ◽  
Min Proteins

ABSTRACT Division site selection is a vital process to ensure generation of viable offspring. In many rod-shaped bacteria, a dynamic protein system, termed the Min system, acts as a central regulator of division site placement. The Min system is best studied in Escherichia coli, where it shows a remarkable oscillation from pole to pole with a time-averaged density minimum at midcell. Several components of the Min system are conserved in the Gram-positive model organism Bacillus subtilis. However, in B. subtilis, it is commonly believed that the system forms a stationary bipolar gradient from the cell poles to midcell. Here, we show that the Min system of B. subtilis localizes dynamically to active sites of division, often organized in clusters. We provide physical modeling using measured diffusion constants that describe the observed enrichment of the Min system at the septum. Mathematical modeling suggests that the observed localization pattern of Min proteins corresponds to a dynamic equilibrium state. Our data provide evidence for the importance of ongoing septation for the Min dynamics, consistent with a major role of the Min system in controlling active division sites but not cell pole areas. IMPORTANCE The molecular mechanisms that help to place the division septum in bacteria is of fundamental importance to ensure cell proliferation and maintenance of cell shape and size. The Min protein system, found in many rod-shaped bacteria, is thought to play a major role in division site selection. It was assumed that there are strong differences in the functioning and in the dynamics of the Min system in E. coli and B. subtilis. Most previous attempts to address Min protein dynamics in B. subtilis have been hampered by the use of overexpression constructs. Here, functional fusions to Min proteins have been constructed by allelic exchange and state-of-the-art imaging techniques allowed to unravel an unexpected fast dynamic behavior of the B. subtilis Min system. Our data show that the molecular mechanisms leading to Min protein dynamics are not fundamentally different in E. coli and B. subtilis.

Influence of the nucleoid and the early stages of DNA replication on positioning the division site in Bacillus subtilis

2010 ◽  
Vol 76 (3) ◽  
pp. 634-647 ◽  
Author(s):  
S. Moriya ◽  
R. A. Rashid ◽  
C. D. Andrade Rodrigues ◽  
E. J. Harry
Keyword(s):  
Bacillus Subtilis ◽  
Dna Replication ◽  
Early Stages ◽  
Division Site

scholarly journals Membrane Redistribution of the Escherichia coli MinD Protein Induced by MinE

2000 ◽  
Vol 182 (3) ◽  
pp. 613-619 ◽  
Author(s):  
S. L. Rowland ◽  
X. Fu ◽  
M. A. Sayed ◽  
Y. Zhang ◽  
W. R. Cook ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Distribution Pattern ◽  
The Other ◽  
Dependent Manner ◽  
Division Site ◽  
Min Proteins ◽  
Selection Of

ABSTRACT Escherichia coli cells contain potential division sites at midcell and adjacent to the cell poles. Selection of the correct division site at midcell is controlled by three proteins: MinC, MinD, and MinE. It has previously been shown (D. Raskin and P. de Boer, Cell 91:685–694, 1997) that MinE-Gfp localizes to the midcell site in an MinD-dependent manner. We use here Gfp-MinD to show that MinD associates with the membrane around the entire periphery of the cell in the absence of the other Min proteins and that MinE is capable of altering the membrane distribution pattern of Gfp-MinD. Studies with the isolated N-terminal and C-terminal MinE domains indicated different roles for the two MinE domains in the redistribution of membrane-associated MinD.

scholarly journals Harnessing β-Lactam Antibiotics for Illumination of the Activity of Penicillin-Binding Proteins in Bacillus subtilis

2019 ◽  
Author(s):  
Shabnam Sharifzadeh ◽  
Felix Dempwolff ◽  
Daniel B. Kearns ◽  
Erin E. Carlson
Keyword(s):  
Bacillus Subtilis ◽  
Binding Proteins ◽  
Single Cells ◽  
Growth Cycle ◽  
Chemical Probes ◽  
Selective Inhibitors ◽  
Penicillin Binding Proteins ◽  
Peptidoglycan Biosynthesis ◽  
Division Site ◽  
Almost All

ABSTRACTSelective chemical probes enable individual investigation of penicillin-binding proteins (PBPs) and provide critical information about their enzymatic activity with spatial and temporal resolution. To identify scaffolds for novel probes to study peptidoglycan biosynthesis in Bacillus subtilis, we evaluated the PBP inhibition profiles of 21 β-lactam antibiotics from different structural subclasses using a fluorescence-based assay. Most compounds readily labeled PBP1, PBP2a, PBP2b or PBP4. Almost all penicillin scaffolds were co-selective for all or combinations of PBP2a, 2b and 4. Cephalosporins, on the other hand, possessed the lowest IC50 values for PBP1 alone or along with PBP4 (ceftriaxone, cefoxitin), 2b (cefotaxime) or 2a, 2b and 4 (cephalothin). Overall, five selective inhibitors for PBP1 (aztreonam, faropenem, piperacillin, cefuroxime and cefsulodin), one selective inhibitor for PBP5 (6-aminopenicillanic acid) and various co-selective inhibitors for other PBPs in B. subtilis were discovered. Surprisingly, carbapenems strongly inhibited PBP3, formerly shown to have low affinity for β-lactams and speculated to be involved in resistance in B. subtilis. To investigate the specific roles of PBP3, we developed activity-based probes based on the meropenem core and utilized them to monitor the activity of PBP3 in living cells. We showed that PBP3 activity localizes as patches in single cells and concentrates as a ring at the septum and the division site during the cell growth cycle. Our activity-based approach enabled spatial resolution of the transpeptidation activity of individual PBPs in this model microorganism, which was not possible with previous chemical and biological approaches.

scholarly journals The Min-protein oscillations in Escherichia coli : an example of self-organized cellular protein waves

2018 ◽  
Vol 373 (1747) ◽  
pp. 20170111 ◽  
Author(s):  
Lukas Wettmann ◽  
Karsten Kruse
Keyword(s):  
Escherichia Coli ◽  
Cell Biology ◽  
Experimental Studies ◽  
Cellular Protein ◽  
Self Organization ◽  
Division Site ◽  
Min Proteins ◽  
Spatio Temporal

In the rod-shaped bacterium Escherichia coli , selection of the cell centre as the division site involves pole-to-pole oscillations of the proteins MinC, MinD and MinE. This spatio-temporal pattern emerges from interactions among the Min proteins and with the cytoplasmic membrane. Combining experimental studies in vivo and in vitro together with theoretical analysis has led to a fairly good understanding of Min-protein self-organization. In different geometries, the system can, in addition to standing waves, also produce travelling planar and spiral waves as well as coexisting stable stationary distributions. Today it stands as one of the best-studied examples of cellular self-organization of proteins. This article is part of the theme issue ‘Self-organization in cell biology’.

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