scholarly journals Linking the Peptidoglycan Synthesis Protein Complex with Asymmetric Cell Division during Bacillus subtilis Sporulation

2020 ◽  
Vol 21 (12) ◽  
pp. 4513 ◽  
Author(s):  
Katarína Muchová ◽  
Zuzana Chromiková ◽  
Imrich Barák
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Protein Complex ◽  
Asymmetric Cell Division ◽  
Morphological Changes ◽  
Direct Interaction ◽  
Specific Protein ◽  
Peptidoglycan Biosynthesis ◽  
Peptidoglycan Synthesis ◽  
Septum Formation

Peptidoglycan is generally considered one of the main determinants of cell shape in bacteria. In rod-shaped bacteria, cell elongation requires peptidoglycan synthesis to lengthen the cell wall. In addition, peptidoglycan is synthesized at the division septum during cell division. Sporulation of Bacillus subtilis begins with an asymmetric cell division. Formation of the sporulation septum requires almost the same set of proteins as the vegetative septum; however, these two septa are significantly different. In addition to their differences in localization, the sporulation septum is thinner and it contains SpoIIE, a crucial sporulation specific protein. Here we show that peptidoglycan biosynthesis is linked to the cell division machinery during sporulation septum formation. We detected a direct interaction between SpoIIE and GpsB and found that both proteins co-localize during the early stages of asymmetric septum formation. We propose that SpoIIE is part of a multi-protein complex which includes GpsB, other division proteins and peptidoglycan synthesis proteins, and could provide a link between the peptidoglycan synthesis machinery and the complex morphological changes required for forespore formation during B. subtilis sporulation.

scholarly journals Sporulation in Bacillus subtilis. Correlation of biochemical events with morphological changes in asporogeneous mutants

1970 ◽  
Vol 118 (4) ◽  
pp. 667-676 ◽  
Author(s):  
W. M. Waites ◽  
D. Kay ◽  
I. W. Dawes ◽  
D. A. Wood ◽  
S. C. Warren ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Subtilis ◽  
Cell Division ◽  
Biochemical Marker ◽  
Morphological Changes ◽  
Glucose Dehydrogenase ◽  
Stage Iv ◽  
The Other ◽  
Stage Ii ◽  
Stage Iii

A comparison was made of morphological changes and successive, mainly biochemical, marker events for sporulation in 14 asporogenous mutants. The morphological and biochemical sequences are linked so that arrested development in one is accompanied by corresponding effects in the other. Thus mutants that fail to produce both protease and antibiotic do not progress beyond stage 0, formation of alkaline phosphatase appears to be associated with the transition from stage II to stage III and glucose dehydrogenase with that from stage III to stage IV. Stage II mutants may produce `pygmy' cells or other bizarre cell-division forms. The biochemical sequence is dependent in the sense that if the occurrence of any one event is blocked that of all the succeeding events is also blocked. This has implications for biochemical models that have been proposed to explain the temporal sequence observed in spore development.

scholarly journals Partitioning of Chromosomal DNA during Establishment of Cellular Asymmetry in Bacillus subtilis

2002 ◽  
Vol 184 (6) ◽  
pp. 1743-1749 ◽  
Author(s):  
Joe Pogliano ◽  
Marc D. Sharp ◽  
Kit Pogliano
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Asymmetric Cell Division ◽  
Chromosome Structure ◽  
Chromosomal Dna ◽  
Chromosome Partitioning ◽  
Cellular Asymmetry ◽  
The Future ◽  
Asymmetric Partitioning ◽  
Polar Division

ABSTRACT The switch from symmetric to asymmetric cell division is a key feature of development in many organisms, including Bacillus subtilis sporulation. Here we demonstrate that, prior to the onset of asymmetric cell division, the B. subtilis chromosome is partitioned into two unequally sized domains, with the origin-proximal one-third of the future forespore chromosome condensed near one pole of the cell. Asymmetric chromosome partitioning is independent of polar division, as it occurs in cells depleted of FtsZ but depends on two transcription factors that govern the initiation of sporulation, σH and Spo0A-P. It is also independent of chromosome partitioning proteins Spo0J and Soj, suggesting the existence of a novel mechanism controlling chromosome structure. Thus, our results demonstrate that, during sporulation, two separable events prepare B. subtilis for asymmetric cell division: the relocation of cell division sites to the cell poles and the asymmetric partitioning of the future forespore chromosome.

scholarly journals Numb-Associated Kinase Interacts with the Phosphotyrosine Binding Domain of Numb and Antagonizes the Function of Numb In Vivo

1998 ◽  
Vol 18 (1) ◽  
pp. 598-607 ◽  
Author(s):  
Cheng-ting Chien ◽  
Shuwen Wang ◽  
Michael Rothenberg ◽  
Lily Y. Jan ◽  
Yuh Nung Jan
Keyword(s):  
Cell Division ◽  
Cell Fate ◽  
Asymmetric Cell Division ◽  
Gene Dosage ◽  
Specific Protein ◽  
Physical Interaction ◽  
Protein Protein Interaction ◽  
Phosphotyrosine Binding Domain ◽  
Ptb Domain

ABSTRACT During asymmetric cell division, the membrane-associated Numb protein localizes to a crescent in the mitotic progenitor and is segregated predominantly to one of the two daughter cells. We have identified a putative serine/threonine kinase, Numb-associated kinase (Nak), which interacts physically with the phosphotyrosine binding (PTB) domain of Numb. The PTB domains of Shc and insulin receptor substrate bind to an NPXY motif which is not present in the region of Nak that interacts with Numb PTB domain. We found that the Numb PTB domain but not the Shc PTB domain interacts with Nak through a peptide of 11 amino acids, implicating a novel and specific protein-protein interaction. Overexpression of Nak in the sensory organs causes both daughters of a normally asymmetric cell division to adopt the same cell fate, a transformation similar to the loss of numb function phenotype and opposite the cell fate transformation caused by overexpression of Numb. The frequency of cell fate transformation is sensitive to the numb gene dosage, as expected from the physical interaction between Nak and Numb. These findings indicate that Nak may play a role in cell fate determination during asymmetric cell divisions.

scholarly journals Asymmetric localization of the cell division machinery during Bacillus subtilis sporulation

2020 ◽  
Author(s):  
Kanika Khanna ◽  
Javier López-Garrido ◽  
Joseph Sugie ◽  
Kit Pogliano ◽  
Elizabeth Villa
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Vegetative Growth ◽  
Bacterial Cell ◽  
Mother Cell ◽  
Electron Tomography ◽  
Leading Edge ◽  
Specific Protein ◽  
Bacterial Cell Division ◽  
Division Plane

The mechanistic details of bacterial cell division are poorly understood. The Gram-positive bacterium Bacillus subtilis can divide via two modes. During vegetative growth, the division septum is formed at the mid cell to produce two equal daughter cells. However, during sporulation, the division septum is formed closer to one pole to yield a smaller forespore and a larger mother cell. We use cryo-electron tomography to visualize the architectural differences in the organization of FtsAZ filaments, the major orchestrators of bacterial cell division during these conditions. We demonstrate that during vegetative growth, FtsAZ filaments are present uniformly around the leading edge of the invaginating septum but during sporulation, they are only present on the mother cell side. Our data show that the sporulation septum is thinner than the vegetative septum during constriction, and that this correlates with half as many FtsZ filaments tracking the division plane during sporulation as compared to vegetative growth. We further find that a sporulation-specific protein, SpoIIE, regulates divisome localization and septal thickness during sporulation. Our data provide first evidence of asymmetric localization of the cell division machinery, and not just septum formation, to produce different cell types with diverse fates in bacteria.

scholarly journals DivIVA Is Required for Polar Growth in the MreB-Lacking Rod-Shaped Actinomycete Corynebacterium glutamicum

2008 ◽  
Vol 190 (9) ◽  
pp. 3283-3292 ◽  
Author(s):  
Michal Letek ◽  
Efrén Ordóñez ◽  
José Vaquera ◽  
William Margolin ◽  
Klas Flärdh ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Division ◽  
Streptococcus Pneumoniae ◽  
Corynebacterium Glutamicum ◽  
Chromosome Segregation ◽  
Polar Growth ◽  
Cell Wall Synthesis ◽  
Peptidoglycan Synthesis ◽  
Polarized Cell Growth

ABSTRACT The actinomycete Corynebacterium glutamicum grows as rod-shaped cells by zonal peptidoglycan synthesis at the cell poles. In this bacterium, experimental depletion of the polar DivIVA protein (DivIVACg) resulted in the inhibition of polar growth; consequently, these cells exhibited a coccoid morphology. This result demonstrated that DivIVA is required for cell elongation and the acquisition of a rod shape. DivIVA from Streptomyces or Mycobacterium localized to the cell poles of DivIVACg-depleted C. glutamicum and restored polar peptidoglycan synthesis, in contrast to DivIVA proteins from Bacillus subtilis or Streptococcus pneumoniae, which localized at the septum of C. glutamicum. This confirmed that DivIVAs from actinomycetes are involved in polarized cell growth. DivIVACg localized at the septum after cell wall synthesis had started and the nucleoids had already segregated, suggesting that in C. glutamicum DivIVA is not involved in cell division or chromosome segregation.

scholarly journals FtsA Mutants of Bacillus subtilis Impaired in Sporulation

2002 ◽  
Vol 184 (14) ◽  
pp. 3856-3863 ◽  
Author(s):  
Jennifer T. Kemp ◽  
Adam Driks ◽  
Richard Losick
Keyword(s):  
Electron Microscopy ◽  
Bacillus Subtilis ◽  
Cell Division ◽  
Amino Acid ◽  
Fluorescence Microscopy ◽  
Protein Interaction ◽  
Regulatory Protein ◽  
Specific Protein ◽  
Morphological Process ◽  
Polar Division

ABSTRACT Spore formation in Bacillus subtilis involves a switch in the site of cell division from the midcell to a polar position. Both medial division and polar division are mediated in part by the actin-like, cytokinetic protein FtsA. We report the isolation of an FtsA mutant (FtsAD265G) that is defective in sporulation but is apparently unimpaired in vegetative growth. Sporulating cells of the mutant reach the stage of asymmetric division but are partially blocked in the subsequent morphological process of engulfment. As judged by fluorescence microscopy and electron microscopy, the FtsAD265G mutant produces normal-looking medial septa but immature (abnormally thin) polar septa. The mutant was unimpaired in transcription under the control of Spo0A, the master regulator for entry into sporulation, but was defective in transcription under the control of σF, a regulatory protein whose activation is known to depend on polar division. An amino acid substitution at a residue (Y264) adjacent to D265 also caused a defect in sporulation. D265 and Y264 are conserved among endospore-forming bacteria, raising the possibility that these residues are involved in a sporulation-specific protein interaction that facilitates maturation of the sporulation septum and the activation of σF.

scholarly journals Asymmetric localization of the cell division machinery during Bacillus subtilis sporulation

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Kanika Khanna ◽  
Javier Lopez Garrido ◽  
Joseph Sugie ◽  
Kit Pogliano ◽  
Elizabeth Villa
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Mother Cell ◽  
Electron Tomography ◽  
Leading Edge ◽  
Specific Protein ◽  
Bacterial Cell Division ◽  
Daughter Cells ◽  
Septal Thickness ◽  
Cryo Electron Tomography

The Gram-positive bacterium Bacillus subtilis can divide via two modes. During vegetative growth, the division septum is formed at the midcell to produce two equal daughter cells. However, during sporulation, the division septum is formed closer to one pole to yield a smaller forespore and a larger mother cell. Using cryo-electron tomography, genetics and fluorescence microscopy, we found that the organization of the division machinery is different in the two septa. While FtsAZ filaments, the major orchestrators of bacterial cell division, are present uniformly around the leading edge of the invaginating vegetative septa, they are only present on the mother cell side of the invaginating sporulation septa. We provide evidence suggesting that the different distribution and number of FtsAZ filaments impact septal thickness, causing vegetative septa to be thicker than sporulation septa already during constriction. Finally, we show that a sporulation-specific protein, SpoIIE, regulates asymmetric divisome localization and septal thickness during sporulation.

scholarly journals Agrobacterium tumefaciensdivisome proteins regulate the transition from polar growth to cell division

2018 ◽  
Author(s):  
Matthew Howell ◽  
Alena Aliashkevich ◽  
Kousik Sundararajan ◽  
Jeremy J. Daniel ◽  
Patrick J. Lariviere ◽  
...  
Keyword(s):  
Cell Division ◽  
Cell Separation ◽  
Cell Depletion ◽  
Polar Growth ◽  
Gtpase Activity ◽  
Peptidoglycan Biosynthesis ◽  
Peptidoglycan Synthesis

AbstractThe mechanisms that restrict peptidoglycan biosynthesis to the pole during elongation and re-direct peptidoglycan biosynthesis to mid-cell during cell division in polar-growing Alphaproteobacteria are largely unknown. Here, we demonstrate that although two of the three FtsZ homologs localize to mid-cell, exhibit GTPase activity and form co-polymers, only one, FtsZAT, is required for cell division. We find that FtsZATis required not only for constriction and cell separation, but also for the termination of polar growth and regulation of peptidoglycan synthesis at mid-cell. Depletion of FtsZ inA. tumefacienscauses a striking phenotype: cells are extensively branched and accumulate growth active poles through tip splitting events. When cell division is blocked at a later stage, polar growth is terminated and ectopic growth poles emerge from mid-cell. Overall, this work suggests thatA. tumefaciensFtsZ makes distinct contributions to the regulation of polar growth and cell division.

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