Analysis of Bacterial Filamentous Temperature-Sensitive Z

Our experts have a keen interest in the study of liquid-liquid and liquid-solid phase transitions in bacterial cells. We have cutting-edge super-resolution imaging or infinite diffraction microscopy apparently combined with single molecule trafficking methods, and computer analysis platforms to analyze key microbial biomolecular condensates undergoing LLPS, as well as the formation and organization of biomolecular condensates within the intracellular space. Here, CD BioSciences is committed to analyzing intrinsically disordered bacterial filamentous temperature-sensitive Z (FtsZ).

FtsZ as a Bacterial Biomolecular Condensate

FtsZ is a soluble GTPase, a bacterial microtubulin homolog that acts as the central element of the division loop in most bacteria and many archaea. FtsZ contains and/or interacts with other concomitant division elements that display key molecular features similar to those that drive phase separation in eukaryotic cells. The C-terminal junction of FtsZ has long been recognized as an intrinsically disordered peptide (IDP) and functions as a flexible tether that attaches FtsZ protofilaments to the cell membrane. When bacterial cells are ready to divide, FtsZ self-assembles in the mid-cell region into a dynamic structure called the Z-loop, which is responsible for the assembly of schizonts and peptidoglycan synthetic complexes at the site of cell division.

Fig. 1. Structure of FtsZ protein. (Battaje R R, et al., 2023)

Customized Services

FtsZ formation condensates provide the cytoskeletal framework and contractile force for bacterial cell division. We provide two model organisms, the rod-shaped bacteria Bacillus subtilis and Escherichia coli, as well as a number of other pathogenic bacteria (e.g., Staphylococcus aureus, Streptococcus pneumoniae, Mycobacterium tuberculosis, and Pseudomonas aeruginosa) to characterize the structure and function of FtsZ. Our research focus area is the kinetics of FtsZ and its regulation within the cell.

CD BioSciences provides specialized services to analyze the structural dynamics and biochemical functions of intrinsically disordered FtsZ in different bacteria. Our services include:

• Characterization of FtsZ in Vitro
  The C-terminus of FtsZ is an important structural domain for the formation of active sites. We offer AlphaFold for AI predictive modeling of the structure of FtsZ C-terminal tail region in different bacteria. We further can detect the structure of the C-terminal tail in vitro by circular dichroism and trypsin protein hydrolysis. In addition, we provide dynamic light scattering (DLS) measurements of different Bs- for assessing the contribution of non-natural intermolecular interactions between FtsZ protomers of FtsZ variants.
• Characterization of FtsZ in Vivo
  In order to examine the role of the C-terminal tail of FtsZ, our technical team can make many variants and test their ability to act on cell division. The specific process is as follows:
  (1) First, we can construct over 35 different C-terminal tail structures using the original pJSB-EcFtsZ plasmid and test their complementarity.
  (2) In vivo testing of EcFtsZ junctions with C-terminal tails from other bacterial species as well as IDP exchanges from unrelated proteins.
  (3) We use immunofluorescence microscopy (IFM) to quantify cell length and image FtsZ ring formation to help you analyze the FtsZ assembly in vivo.
• Determine the Functional Role of Different RNA Degradosomal Proteins on mRNA Decay
  Disrupting the tight regulation of bacterial cell division has been identified as an attractive strategy for the discovery of novel antibiotics. We developed targeting FtsZ as a very useful antimicrobial therapeutic strategy by interfering with its GTPase activity or Z-loop assembly/disassembly kinetics, or by disrupting the structural integrity of FtsZ leading to its degradation. Our experts are committed to developing broad-spectrum antibiotics targeting FtsZ.

CD BioSciences offers a simple modular biomolecular platform to characterize the LLPS of intrinsically disordered FtsZ. We aim to use pathogenic bacteria as representatives to analyze the structure and function of FtsZ and its potential as an antibiotic target. If you have any special requirements for our services, please feel free to contact us.