scholarly journals The Bacillus subtilis division protein DivIC is a highly abundant membrane‐bound protein that localizes to the division site

1997 ◽  
Vol 26 (5) ◽  
pp. 1047-1055 ◽  
Author(s):  
V. L. Katis ◽  
E. J. Harry ◽  
R. G. Wake
Keyword(s):  
Bacillus Subtilis ◽  
Division Site ◽  
Membrane Bound

scholarly journals Septal Localization of the Membrane-Bound Division Proteins ofBacillus subtilis DivIB and DivIC Is Codependent Only at High Temperatures and Requires FtsZ

2000 ◽  
Vol 182 (12) ◽  
pp. 3607-3611 ◽  
Author(s):  
V. L. Katis ◽  
R. G. Wake ◽  
E. J. Harry
Keyword(s):  
Bacillus Subtilis ◽  
High Temperatures ◽  
Immunofluorescence Microscopy ◽  
High Growth ◽  
Specific Role ◽  
Ofbacillus Subtilis ◽  
Division Site ◽  
Membrane Bound ◽  
Septal Localization

ABSTRACT Using immunofluorescence microscopy, we have examined the dependency of localization among three Bacillus subtilisdivision proteins, FtsZ, DivIB, and DivIC, to the division site. DivIC is required for DivIB localization. However, DivIC localization is dependent on DivIB only at high growth temperatures, at which DivIB is essential for division. FtsZ localization is required for septal recruitment of DivIB and DivIC, but FtsZ can be recruited independently of DivIB. These localization studies suggest a more specific role for DivIB in division, involving interaction with DivIC.

scholarly journals Cell Division in Bacillus subtilis: FtsZ and FtsA Association Is Z-Ring Independent, and FtsA Is Required for Efficient Midcell Z-Ring Assembly

2005 ◽  
Vol 187 (18) ◽  
pp. 6536-6544 ◽  
Author(s):  
S. O. Jensen ◽  
L. S. Thompson ◽  
E. J. Harry
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Ring Formation ◽  
Division Site ◽  
Ring Assembly ◽  
Synchronous Cell ◽  
Z Ring ◽  
Membrane Bound ◽  
Chemical Cross Linking

ABSTRACT The earliest stage in cell division in bacteria is the assembly of a Z ring at the division site at midcell. Other division proteins are also recruited to this site to orchestrate the septation process. FtsA is a cytosolic division protein that interacts directly with FtsZ. Its function remains unknown. It is generally believed that FtsA localization to the division site occurs immediately after Z-ring formation or concomitantly with it and that FtsA is responsible for recruiting the later-assembling membrane-bound division proteins to the division site. Here, we report the development of an in vivo chemical cross-linking assay to examine the association between FtsZ and FtsA in Bacillus subtilis cells. We subsequently use this assay in a synchronous cell cycle to show that these two proteins can interact prior to Z-ring formation. We further show that in a B. subtilis strain containing an ftsA deletion, FtsZ localized at regular intervals along the filament but the majority of Z rings were abnormal. FtsA in this organism is therefore critical for the efficient formation of functional Z rings. This is the first report of abnormal Z-ring formation resulting from the loss of a single septation protein. These results suggest that in this organism, and perhaps others, FtsA ensures recruitment of the membrane-bound division proteins by ensuring correct formation of the Z ring.

scholarly journals Lipid droplets maintain lipid homeostasis during anaphase for efficient cell separation in budding yeast

2016 ◽  
Vol 27 (15) ◽  
pp. 2368-2380 ◽  
Author(s):  
Po-Lin Yang ◽  
Tzu-Han Hsu ◽  
Chao-Wen Wang ◽  
Rey-Huei Chen
Keyword(s):  
Cell Separation ◽  
Neutral Lipids ◽  
Budding Yeast ◽  
Acid Synthesis ◽  
Mitotic Exit ◽  
Lipid Homeostasis ◽  
Physiological Conditions ◽  
Division Site ◽  
Quadruple Mutant ◽  
Membrane Bound

The neutral lipids steryl ester and triacylglycerol (TAG) are stored in the membrane-bound organelle lipid droplet (LD) in essentially all eukaryotic cells. It is unclear what physiological conditions require the mobilization or storage of these lipids. Here, we study the budding yeast mutant are1Δ are2Δ dga1Δ lro1Δ, which cannot synthesize the neutral lipids and therefore lacks LDs. This quadruple mutant is delayed at cell separation upon release from mitotic arrest. The cells have abnormal septa, unstable septin assembly during cytokinesis, and prolonged exocytosis at the division site at the end of cytokinesis. Lipidomic analysis shows a marked increase of diacylglycerol (DAG) and phosphatidic acid, the precursors for TAG, in the mutant during mitotic exit. The cytokinesis and separation defects are rescued by adding phospholipid precursors or inhibiting fatty acid synthesis, which both reduce DAG levels. Our results suggest that converting excess lipids to neutral lipids for storage during mitotic exit is important for proper execution of cytokinesis and efficient cell separation.

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

Properties of Inosinic Acid Dehydrogenase from Bacillus subtilis. I. Purification and Physical Properties

1973 ◽  
Vol 51 (10) ◽  
pp. 1380-1390 ◽  
Author(s):  
Tai-Wing Wu ◽  
K. G. Scrimgeour
Keyword(s):  
Bacillus Subtilis ◽  
Quaternary Structure ◽  
Active Form ◽  
Kinetic Properties ◽  
Purification Method ◽  
Molecular Weights ◽  
Inosinic Acid ◽  
Apparent Homogeneity ◽  
Catalytically Active ◽  
Membrane Bound

IMP (inosinic acid or inosine-5′-phosphate) dehydrogenase has been purified to apparent homogeneity from Bacillus subtilis. The purification method yields an enzyme preparation that retains a constant level of inhibition by guanosine 5′-phosphate. The enzyme is membrane bound, and can be removed from membrane material after treatment either with detergents or with phospholipase A. Both the membrane-bound and solubilized forms of IMP dehydrogenase have similar kinetic properties. The soluble enzyme can occur in a number of oligomeric forms, with molecular weights that are multiples of 100 000 daltons. Although both the tetramer and the dimer appear to be catalytically active, no conclusions can yet be drawn about the quaternary structure of the enzymically active form(s).

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.

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