Bacterial Tubulin
Bacterial Tubulin - Related Videos
02:40
Second Harmonic Generation Imaging in a Rat Model to Study Tubulin Defects
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2025
Source: Piazza, V., et al., Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin. J. Vis. Exp. (2023)This video demonstrates the procedure for imaging microtubule abnormalities in a rat brain tissue slice using a two-photon excitation microscope. It employs second harmonic generation (SHG) signals to detect tubulin defects and reduced myelin production.
06:30
Optimizing Tubulin Yield from Porcine Brain Tissue
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2024
This protocol describes a technique for the high-yield isolation of tubulin from the porcine brain optimized for small-scale instrumentation. The isolation procedures are complemented by procedures for determining tubulin polymerization activity in vitro using co-sedimentation assays and transmission electron microscopy.
08:07
Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin
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2023
In this article, we present a protocol to detect microtubule-loaded oligodendrocytes in a model of tubulinopathy through a simple, innovative second harmonic generation microscopy approach.
05:21
Bacterial Transformation - Student Protocol
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2019
Bacterial Transformation ExpandIMPORTANT: In addition to wearing the appropriate personal protective equipment, be sure to take care to keep your face away from suspension cultures, and to avoid inhaling reagents. Do not touch your face while performing the experiment. Always wash your hands before and after every experiment. When you are ready to safely begin, check to make sure you have a tube or tubes of competent E. coli cells in your ice bucket. Then, transfer 50 µL from one of these tubes...
03:57
Bacterial Infection Quantitation Assay: A Method to Quantify Intraocular Bacterial Load in Mouse Model of Bacterial Endophthalmitis
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2025
This video describes the technique of quantifying bacterial infection from eye homogenates obtained from a murine model of bacterial endophthalmitis caused by Bacillus cereus. This technique helps study the host immune response and its dependency on the host and ocular bacterial gene expression in murine models.
FAQs
In organisms such as Prosthecobacter, BtubA and BtubB associate as heterodimers, meaning two different protein subunits function together. These heterodimers bind GTP and then polymerize into microtubule-like filaments. Because the proteins can also undergo disassembly, the resulting structures are dynamic rather than permanently fixed, allowing bacterial organization to be linked to regulated protein assembly.
GTP binding is associated with the assembly behavior of bacterial tubulin. After BtubA and BtubB form heterodimers, GTP supports their polymerization into filaments, while the structures can subsequently disassemble. This reversible behavior matters because it provides a molecular basis for examining how cytoskeletal polymers form, change, and potentially reorganize inside bacterial cells.
Bacterial tubulin provides a comparative system for studying tubulin-like polymers outside eukaryotic cells. Its GTP-dependent assembly and microtubule-like filament formation connect bacterial protein organization with mechanisms associated with microtubules, while its presence in prokaryotes informs questions about cytoskeletal evolution. These comparisons help investigate which organizational features may have emerged early across life.
The filaments provide physical organization within bacterial cells and may contribute to chromosome or cellular positioning. However, the precise function is not identical across species, so structural observation alone does not establish one universal role. Investigators therefore interpret polymer formation alongside the biology of the organism being studied, especially when relating filament location to cellular organization.
A basic assembly study would focus on the behavior of BtubA and BtubB as they associate, bind GTP, polymerize into filaments, and later disassemble. Comparing these stages can reveal how heterodimer formation relates to polymer growth and loss. The resulting observations provide a foundation for connecting molecular assembly with the physical organization seen in bacterial cells.
Prosthecobacter provides an example in which the bacterial tubulin proteins BtubA and BtubB assemble as heterodimers and form dynamic, microtubule-like filaments. This makes the organism relevant for connecting protein-level events with bacterial cell organization. It also offers a biological context for examining how tubulin-like cytoskeletal systems occur in prokaryotes.
Research on bacterial tubulin links molecular evolution, cytoskeletal biology, and protein assembly. It can help clarify how cellular organization evolved across life and provide models for examining mechanisms relevant to microtubules. The system also has potential significance for antimicrobial research, because bacterial cytoskeletal proteins may eventually help identify new targets, although their precise roles vary among species.