The Role of Bola in Bacterial Physiology
The Role of Bola in Bacterial Physiology
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BolA is a FtsZ-dependent gene induced in stationary phase and stress conditions. It was found that its overexpression makes E. coli rod-shaped cells spherical and it acts as a transcription factor modulating cell permeability, biofilm formation and motility.
Unlike conventional amphiphilic molecules with single-headed hydrophilic regions, the bola structure has double-headed hydrophilic groups at its termini, which leads to superior water solubility. Its intrinsic biocompatibility and easy accessibility through traditional peptide synthesis make it an attractive candidate for constructing self-assembling biomaterials and drugs.
What is bola-like?
Bola-like proteins are a large family of genes widespread in prokaryotes and eukaryotes [1]. They were first discovered in E. coli, where their overexpression caused rod-shaped cells to become spherical (hence the name of the protein), and they have since been linked to many different phenotypes. They are often induced during the stationary phase of growth and in response to various stresses.
Gauchos use bolas to capture running cattle and game; they are typically designed with two shorter cords with weights on the end, and one longer cord with a light weight at the nexus of the cords. The weights hit either side of the animal's legs, and the lighter weight wraps around the body and binds its feet. Phylogenetic analyses of gene sequences have revealed that BolA proteins are divided into four subfamilies, based on the -helical domain they contain (see Figure 1). The trees were reconstructed using MEGA software v11.0.11 (14). Bootstrap values are written at the nodes.
What is bola-amphiphile?
Bolaamphiphiles are characterized by Onbola polar heads at opposite ends of the molecule and non-polar tails that can form micelles, rods, tubes and fibers. They have a distinct shape that is inspired by the weapons of South American hunters, hence the name bola (bola=skull).
Bola-like surfactants can be co-solubilized with membrane proteins in detergent-free conditions and are expected to preferentially interact with the TMDs of well-folded MPs. This interaction is expected to dampen chain motion that destabilizes the membrane protein owing to an entropy penalty that is paid when the tails bump up against the TMD surface.
Unlike conventional surfactants, addition of bolaamphiphiles to micellar NMR samples of DAGK does not result in degradation of spectral quality suggesting that these molecules are compatible with structural biology studies. Further, bolaamphiphiles appear to fully solubilize lipids without affecting their folding and are capable of spanning typical La-phase bilayers in tapping-mode AFM experiments.
What is bola-like peptide?
Bola-like metabolites, also known as bolaamphiphiles, are bipolar peptides that have two hydrophobic and non-polar ends. They are widespread in archaea and bacteria and have many different structures. They are characterized by their wide pH range and ability to bind ions such as iron.
The bolA protein is involved in a number of cellular processes, such as cell morphology and biofilm formation. It has been shown that bolA is required for the switch between motile and sessile lifestyle in E. coli and that it regulates FtsZ-dependent cell morphogenesis and flagellar synthesis [1].
Compared to copyright-type amphiphiles, bola-like peptides are usually characterized by two heads with hydrophilic amino acids flanking a hydrophobic core, resulting in improved water solubility and thermal stability. They have also demonstrated good antibacterial activity.
What is bola-like protein?
BolA is a transcription factor that influences many aspects of bacterial cell physiology including biofilm formation, motility and flagella assembly. It was first identified in E. coli as a stationary phase stress-responsive gene that overexpression makes cells spherical, and it was later found to play an important role in the switch between motile and sessile lifestyles, biofilm formation and virulence.
Phylogenetic analysis showed that BolA proteins are conserved across prokaryotes and most eukaryotes, with the exception of photosynthetic organisms. A highly conserved sequence motif is present in all BolA proteins and contains a histidine residue that may function to covalently bind iron from the FeS cluster. In addition, BolA negatively regulates the expression of genes encoding diguanylate cyclases and phosphodiesterases, controls the synthesis of secondary signal metabolite c-di-GMP, induces tricarboxylic acid cycle genes, fimbria-like adhesins and represses the expression of genes encoding flagellar proteins.
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