scholarly journals A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis

2002 ◽  
Vol 47 (1) ◽  
pp. 159-169 ◽  
Author(s):  
Sabine Autret ◽  
Jeffery Errington
Keyword(s):  
Bacillus Subtilis ◽  
Site Selection ◽  
Division Site

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.

A novel component of the division-site selection system ofBacillus subtilisand a new mode of action for the division inhibitor MinCD

2008 ◽  
Vol 70 (6) ◽  
pp. 1556-1569 ◽  
Author(s):  
Marc Bramkamp ◽  
Robyn Emmins ◽  
Louise Weston ◽  
Catriona Donovan ◽  
Richard A. Daniel ◽  
...  
Keyword(s):  
Site Selection ◽  
Mode Of Action ◽  
Selection System ◽  
Division Site

scholarly journals Genetic Dissection of DivIVA Functions in Listeria monocytogenes

2017 ◽  
Vol 199 (24) ◽  
Author(s):  
Karan Gautam Kaval ◽  
Samuel Hauf ◽  
Jeanine Rismondo ◽  
Birgitt Hahn ◽  
Sven Halbedel
Keyword(s):  
Cell Division ◽  
Listeria Monocytogenes ◽  
Protein Interactions ◽  
Site Selection ◽  
Genetic Dissection ◽  
Flagellar Motility ◽  
Content Type ◽  
Division Site ◽  
Interaction Partners ◽  
Species Specific

ABSTRACT DivIVA is a membrane binding protein that clusters at curved membrane regions, such as the cell poles and the membrane invaginations occurring during cell division. DivIVA proteins recruit many other proteins to these subcellular sites through direct protein-protein interactions. DivIVA-dependent functions are typically associated with cell growth and division, even though species-specific differences in the spectrum of DivIVA functions and their causative interaction partners exist. DivIVA from the Gram-positive human pathogen Listeria monocytogenes has at least three different functions. In this bacterium, DivIVA is required for precise positioning of the septum at midcell, it contributes to the secretion of autolysins required for the breakdown of peptidoglycan at the septum after the completion of cell division, and it is essential for flagellar motility. While the DivIVA interaction partners for control of division site selection are well established, the proteins connecting DivIVA with autolysin secretion or swarming motility are completely unknown. We set out to identify divIVA alleles in which these three DivIVA functions could be separated, since the question of the degree to which the three functions of L. monocytogenes DivIVA are interlinked could not be answered before. Here, we identify such alleles, and our results show that division site selection, autolysin secretion, and swarming represent three discrete pathways that are independently influenced by DivIVA. These findings provide the required basis for the identification of DivIVA interaction partners controlling autolysin secretion and swarming in the future. IMPORTANCE DivIVA of the pathogenic bacterium Listeria monocytogenes is a central scaffold protein that influences at least three different cellular processes, namely, cell division, protein secretion, and bacterial motility. How DivIVA coordinates these rather unrelated processes is not known. We here identify variants of L. monocytogenes DivIVA, in which these functions are separated from each other. These results have important implications for the models explaining how DivIVA interacts with other proteins.

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 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 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.

Sign in / Sign up

Export Citation Format

Share Document