Related Experiment Video

Updated: Nov 12, 2025

Fluorescence Live-cell Imaging of the Complete Vegetative Cell Cycle of the Slow-growing Social Bacterium Myxococcus xanthus
11:45

Fluorescence Live-cell Imaging of the Complete Vegetative Cell Cycle of the Slow-growing Social Bacterium Myxococcus xanthus

Published on: June 20, 2018

9.8K

PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus

Dominik Schumacher1, Andrea Harms1, Silke Bergeler2

  • 1Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch, Marburg, Germany.

Elife
|March 18, 2021
PubMed

Insights

The PomX/Y/Z complex in Myxococcus xanthus positions the cell division site. PomX protein has two domains, with the N-terminal domain activating PomZ ATPase and the C-terminal domain scaffolding complex formation and promoting fission.

Area of Science:

  • Microbiology
  • Cell Biology
  • Molecular Biology

Background:

  • Cell division site positioning is crucial for bacterial reproduction but not fully understood.
  • The PomX/Y/Z complex in Myxococcus xanthus is known to position the cytokinetic FtsZ-ring at midcell.
  • This complex translocates across the nucleoid in a PomZ ATPase-dependent manner.

Purpose of the Study:

  • To elucidate the distinct functions of the PomX protein within the PomX/Y/Z complex.
  • To understand the mechanism by which PomX regulates PomZ ATPase activity.
  • To investigate the role of PomX domains in complex formation and fission.

Main Methods:

  • Biochemical assays to assess ATPase activity stimulation.
  • Protein interaction studies to map domain functions.
  • Analysis of PomX/Y/Z complex polymerization and fission dynamics.

Main Results:

  • PomX possesses two functional domains: an N-terminal domain that stimulates PomZ ATPase activity and a C-terminal domain that interacts with PomY.
  • The C-terminal domain of PomX forms polymers, acting as a scaffold for PomX/Y/Z complex assembly.
  • The interaction between PomX and PomZ is essential for the fission of the PomX/Y/Z complex during cell division.

Conclusions:

  • PomX is a modular protein with multiple functions essential for Myxococcus xanthus cell division.
  • The N-terminal domain of PomX activates the PomZ ATPase, similar to other ATPase activating proteins.
  • The C-terminal domain facilitates complex assembly and subsequent fission, highlighting a conserved mechanism in ParA/MinD ATPase regulation.
Keywords:
FtsZMinDMinEParAParBbacterial cell divisioncell biologyinfectious diseasemicrobiology

More Related Videos

Recording Multicellular Behavior in Myxococcus xanthus Biofilms using Time-lapse Microcinematography10:59

Recording Multicellular Behavior in Myxococcus xanthus Biofilms using Time-lapse Microcinematography

Published on: August 6, 2010

12.5K
Visualization of Twitching Motility and Characterization of the Role of the PilG in Xylella fastidiosa08:44

Visualization of Twitching Motility and Characterization of the Role of the PilG in Xylella fastidiosa

Published on: April 8, 2016

11.1K

Related Concept Videos

Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
4.8K
Molecular Factors Affecting Cell Division01:27

Molecular Factors Affecting Cell Division

Several external and internal factors influence the initiation and inhibition of cell division. For instance, the death of nearby cells or the release of human growth hormone (hGH) promotes cell division. In contrast, lack of hGH or crowding of cells can inhibit cell division.
Several proteins function as internal regulators to ensure each cell cycle stage is completed faithfully before proceeding to the next. Regulator molecules may act directly or influence the activity or production of other...
3.6K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
6.0K
Cell Motility through Blebbing01:16

Cell Motility through Blebbing

Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
In multicellular...
2.2K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
5.3K
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.5K