PlpA, a PilZ-like protein, regulates directed motility of the bacterium Myxococcus xanthus

Connor B Pogue1, Tianyi Zhou1, Beiyan Nan1

  • 1Department of Biology, Texas A&M University, College Station, TX 77843, USA.

Molecular Microbiology
|November 12, 2017
PubMed

Insights

Researchers discovered PlpA, a protein regulating bacterial movement direction in Myxococcus xanthus. PlpA and MglA proteins interact to control cell motility and direction, preventing frequent reversals.

Area of Science:

  • Microbiology
  • Cell Biology
  • Bacterial Motility

Background:

  • Myxococcus xanthus exhibits directional movement and regular reversals.
  • Asymmetric localization of Ras-like GTPase MglA is thought to determine cell direction.
  • MglA's symmetric localization in mutants still allows motility, indicating other regulators exist.

Purpose of the Study:

  • Identify novel regulators of Myxococcus xanthus motility direction.
  • Investigate the role of PlpA in controlling cell movement and reversals.
  • Elucidate the interaction between PlpA and MglA in regulating motility.

Main Methods:

  • Genetic analysis of Myxococcus xanthus mutants.
  • Protein localization studies using microscopy.
  • Single motor particle tracking to analyze motility dynamics.

Main Results:

  • PlpA, a PilZ-like protein, was identified as a motility regulator.
  • PlpA and MglA exhibit opposing asymmetric localization patterns.
  • PlpA deletion disrupts MglA asymmetry, increases reversals, and impairs motility.
  • PlpA and MglA directly interact with the gliding motor, with PlpA inhibiting and MglA promoting motor reversal.

Conclusions:

  • PlpA is a key regulator of Myxococcus xanthus motility direction.
  • PlpA and MglA form a regulatory system controlling gliding motor reversal.
  • PlpA stabilizes motility direction by counteracting MglA at lagging cell poles.

Related Concept Videos

Fimbriae, Pili, and Axial Filaments01:28

Fimbriae, Pili, and Axial Filaments

Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
1.0K
Bacterial Phylum Tenericutes01:24

Bacterial Phylum Tenericutes

The phylum Tenericutes, which includes the single class Mollicutes, comprises bacteria that lack cell walls. The term "Mollicutes" derives from the Latin word mollis, meaning "soft." These organisms are among the smallest known and are commonly referred to as mycoplasmas due to the prominence of the genus Mycoplasma, which includes well-known human pathogens. Despite their inability to stain gram-positively (a result of their lack of cell walls), mycoplasmas are phylogenetically related to the...
254
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.8K
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.9K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.3K
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
2.8K