scholarly journals Establishing Rod-Shape from Spherical, Peptidoglycan-Deficient Bacterial Spores

2019 ◽  
Author(s):  
Huan Zhang ◽  
Garrett A. Mulholland ◽  
Sofiene Seef ◽  
Shiwei Zhu ◽  
Jun Liu ◽  
...  
Keyword(s):  
Molecular Motors ◽  
De Novo ◽  
Molecular Motor ◽  
Myxococcus Xanthus ◽  
Negative Bacterium ◽  
Gram Negative ◽  
Spherical Surfaces ◽  
Rod System ◽  
The Status ◽  
Ras Family

ABSTRACTChemical-induced spores of the Gram-negative bacterium Myxococcus xanthus are peptidoglycan (PG)-deficient. It is unclear how these spherical spores germinate into rod-shaped, walled cells without preexisting PG templates. We found that germinating spores first synthesize PG randomly on spherical surfaces. MglB, a GTPase-activating protein, forms a cluster that surveys the status of PG growth and stabilizes at one future cell pole. Following MglB, the Ras family GTPase MglA localizes to the second pole. MglA directs molecular motors to transport the bacterial actin homolog MreB and the Rod PG synthesis complexes away from poles. The Rod system establishes rod-shape by elongating PG at nonpolar regions. Thus, the interaction between GTPase, cytoskeletons and molecular motors provides a mechanism for the de novo establishment of rod-shape in bacteria.SignificanceSpheres and rods are among the most common shapes adopted by walled bacteria, in which the peptidoglycan (PG) cell wall largely determines cell shape. When induced by chemicals, rod-shaped vegetative cells of the Gram-negative bacterium Myxococcus xanthus thoroughly degrade their PG and shrink into spherical spores. As these spores germinate, rod-shaped cells are rebuilt without preexisting templates, which provides a rare opportunity to visualize de novo PG synthesis and bacterial morphogenesis. In this study, we investigated how spherical spores germinate into rods and elucidated a system for rod-shape morphogenesis that includes the Rod PG synthesis system, a GTPase-GAP pair, the MreB cytoskeleton and a molecular motor.

scholarly journals Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores

2020 ◽  
Vol 117 (25) ◽  
pp. 14444-14452
Author(s):  
Huan Zhang ◽  
Garrett A. Mulholland ◽  
Sofiene Seef ◽  
Shiwei Zhu ◽  
Jun Liu ◽  
...  
Keyword(s):  
Molecular Motors ◽  
De Novo ◽  
Eukaryotic Cells ◽  
Bacterial Spores ◽  
Negative Bacterium ◽  
Gtpase Activating Protein ◽  
Spherical Surfaces ◽  
Rod System ◽  
The Status ◽  
Ras Family

Chemical-induced spores of the Gram-negative bacteriumMyxococcus xanthusare peptidoglycan (PG)-deficient. It is unclear how these spherical spores germinate into rod-shaped, walled cells without preexisting PG templates. We found that germinating spores first synthesize PG randomly on spherical surfaces. MglB, a GTPase-activating protein, forms a cluster that responds to the status of PG growth and stabilizes at one future cell pole. Following MglB, the Ras family GTPase MglA localizes to the second pole. MglA directs molecular motors to transport the bacterial actin homolog MreB and the Rod PG synthesis complexes away from poles. The Rod system establishes rod shape de novo by elongating PG at nonpolar regions. Thus, similar to eukaryotic cells, the interactions between GTPase, cytoskeletons, and molecular motors initiate spontaneous polarization in bacteria.

scholarly journals Myxococcus xanthus as a Model Organism for Peptidoglycan Assembly and Bacterial Morphogenesis

2021 ◽  
Vol 9 (5) ◽  
pp. 916
Author(s):  
Huan Zhang ◽  
Srutha Venkatesan ◽  
Beiyan Nan
Keyword(s):  
De Novo ◽  
Myxococcus Xanthus ◽  
Model Organism ◽  
Life Stages ◽  
Negative Bacterium ◽  
Ideal Model ◽  
Daughter Cells ◽  
Bacterial Division ◽  
Cell Shapes ◽  
Rare Opportunity

A fundamental question in biology is how cell shapes are genetically encoded and enzymatically generated. Prevalent shapes among walled bacteria include spheres and rods. These shapes are chiefly determined by the peptidoglycan (PG) cell wall. Bacterial division results in two daughter cells, whose shapes are predetermined by the mother. This makes it difficult to explore the origin of cell shapes in healthy bacteria. In this review, we argue that the Gram-negative bacterium Myxococcus xanthus is an ideal model for understanding PG assembly and bacterial morphogenesis, because it forms rods and spheres at different life stages. Rod-shaped vegetative cells of M. xanthus can thoroughly degrade their PG and form spherical spores. As these spores germinate, cells rebuild their PG and reestablish rod shape without preexisting templates. Such a unique sphere-to-rod transition provides a rare opportunity to visualize de novo PG assembly and rod-like morphogenesis in a well-established model organism.

Multicopy single-stranded DNA isolated from a gram-negative bacterium, Myxococcus xanthus

Cell ◽  
1984 ◽  
Vol 38 (1) ◽  
pp. 203-209 ◽  
Author(s):  
Thomas Yee ◽  
Teiichi Furuichi ◽  
Sumiko Inouye ◽  
Masayori Inouye
Keyword(s):  
Myxococcus Xanthus ◽  
Negative Bacterium ◽  
Single Stranded Dna ◽  
Gram Negative

scholarly journals Myxococcus xanthus as a Model Organism for Peptidoglycan Assembly and Bacterial Morphogenesis

2021 ◽  
Author(s):  
Huan Zhang ◽  
Srutha Venkatesan ◽  
Beiyan Nan
Keyword(s):  
De Novo ◽  
Myxococcus Xanthus ◽  
Model Organism ◽  
Life Stages ◽  
Negative Bacterium ◽  
Ideal Model ◽  
Daughter Cells ◽  
Bacterial Division ◽  
Cell Shapes ◽  
Rare Opportunity

A fundamental question in biology is how cell shapes are genetically encoded and enzymatically generated. Prevalent shapes among walled bacteria include spheres and rods. These shapes are chiefly determined by the peptidoglycan (PG) cell wall. Bacterial division results in two daughter cells, whose shapes are predetermined by the mother. This makes it difficult to explore the origin of cell shapes in healthy bacteria. In this review, we argue that the Gram-negative bacterium Myxococcus xanthus is an ideal model for understanding PG assembly and bacterial morphogenesis because it forms rods and spheres at different life stages. Rod-shaped vegetative cells of M. xanthus can thoroughly degrade their PG and form spherical spores. As these spores germinate, cells rebuild their PG and reestablish rod shape without preexisting templates. Such a unique sphere-to-rod transition provides a rare opportunity to visualize de novo PG assembly and rod-like morphogenesis in a well-established model organism.

scholarly journals A model of processive walking and slipping of kinesin-8 molecular motors

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ping Xie
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
External Load ◽  
Molecular Motor ◽  
Velocity Versus ◽  
Stick Slip ◽  
Load Dependence ◽  
Chemomechanical Coupling ◽  
Similarities And Differences ◽  
Stick Slip Motion

AbstractKinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.

scholarly journals Massiliamide, a cyclic tetrapeptide with potent tyrosinase inhibitory properties from the Gram-negative bacterium Massilia albidiflava DSM 17472T

2020 ◽  
Author(s):  
Andri Frediansyah ◽  
Jan Straetener ◽  
Heike Brötz-Oesterhelt ◽  
Harald Gross
Keyword(s):  
Absolute Configuration ◽  
Inhibitory Activity ◽  
Liquid Culture ◽  
Spectroscopic Analysis ◽  
2D Nmr ◽  
Negative Bacterium ◽  
Gram Negative ◽  
The Absolute ◽  
Potent Inhibitory Activity ◽  
Cyclic Tetrapeptide

AbstractA cyclic tetrapeptide, designated massiliamide, was isolated from the liquid culture of the Gram-negative bacterium Massilia albidiflava DSM 17472T. The structure was elucidated through extensive spectroscopic analysis, including HR-MS and 1D and 2D NMR experiments. The absolute configuration was determined using the Marfey´s method. Massiliamide showed potent inhibitory activity towards tyrosinase with an IC50 value of 1.15 µM and no cytotoxicity.

scholarly journals Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Thomas V. Heidler ◽  
Karin Ernits ◽  
Agnieszka Ziolkowska ◽  
Rolf Claesson ◽  
Karina Persson
Keyword(s):  
Porphyromonas Gingivalis ◽  
Von Willebrand Factor ◽  
Host Cells ◽  
Negative Bacterium ◽  
Oral Biofilm ◽  
Gram Negative ◽  
Type V ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Fimbrial Protein

AbstractThe Gram-negative bacterium Porphyromonas gingivalis is a secondary colonizer of the oral biofilm and is involved in the onset and progression of periodontitis. Its fimbriae, of type-V, are important for attachment to other microorganisms in the biofilm and for adhesion to host cells. The fimbriae are assembled from five proteins encoded by the mfa1 operon, of which Mfa5 is one of the ancillary tip proteins. Here we report the X-ray structure of the N-terminal half of Mfa5, which reveals a von Willebrand factor domain and two IgG-like domains. One of the IgG-like domains is stabilized by an intramolecular isopeptide bond, which is the first such bond observed in a Gram-negative bacterium. These features make Mfa5 structurally more related to streptococcal adhesins than to the other P. gingivalis Mfa proteins. The structure reported here indicates that horizontal gene transfer has occurred among the bacteria within the oral biofilm.

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