Related Experiment Video

Updated: Jan 29, 2026

Phage-mediated Delivery of Targeted sRNA Constructs to Knock Down Gene Expression in E. coli
08:25

Phage-mediated Delivery of Targeted sRNA Constructs to Knock Down Gene Expression in E. coli

Published on: March 20, 2016

13.0K

The Cold Shock Protein CspB from Mycobacterium tuberculosis Binds to MTS0997 sRNA and MTS1338 sRNA as a Dimer

Natalia Lekontseva1, Alisa Mikhaylina1, Polina Pankratova1

  • 1Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Pushchino, Russia.

International Journal of Molecular Sciences
|January 28, 2026
PubMed

Insights

The cold shock protein CspB from Mycobacterium tuberculosis may act as an RNA chaperone, binding to small regulatory RNAs (sRNAs) to influence gene expression. This interaction could be crucial for mycobacterial pathogenesis.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • RNA chaperones are essential for bacterial RNA biogenesis and function.
  • Small regulatory RNAs (sRNAs) modulate gene expression in response to environmental changes.
  • Mycobacteria lack common RNA chaperones like Hfq and ProQ, despite possessing numerous sRNAs.

Purpose of the Study:

  • To investigate the potential RNA chaperone activity of Mycobacterium tuberculosis CspB.
  • To determine the crystal structure of CspB from M. tuberculosis.
  • To assess the binding affinity of CspB for specific mycobacterial sRNAs.

Main Methods:

  • X-ray crystallography to determine the 3D structure of CspB.
  • Biochemical assays to measure the binding affinity of CspB to MTS0997 and MTS1338 sRNAs.

Main Results:

  • The crystal structure revealed CspB forms a dimer via its C-terminal region.
  • M. tuberculosis CspB demonstrated high-affinity binding to MTS0997 and MTS1338 sRNAs.
  • These findings suggest CspB functions similarly to known RNA chaperones Hfq and ProQ.

Conclusions:

  • CspB from M. tuberculosis possesses RNA chaperone activity.
  • CspB interacts with specific sRNAs in M. tuberculosis.
  • CspB may play a role in regulating mycobacterial pathogenesis through sRNA interactions.
Keywords:
CspBMycobacterium tuberculosisRNA chaperoneRNA–protein interactionscold shock proteinssRNAα-helix hairpin

More Related Videos

Separation and Fractionation of Culture Filtrate Proteins (CFPs) from Mycobacterium tuberculosis08:48

Separation and Fractionation of Culture Filtrate Proteins (CFPs) from Mycobacterium tuberculosis

Published on: July 11, 2025

577
Separation and Fractionation of Cell Wall and Cell Membrane Proteins from Mycobacterium tuberculosis for Downstream Protein Analysis06:14

Separation and Fractionation of Cell Wall and Cell Membrane Proteins from Mycobacterium tuberculosis for Downstream Protein Analysis

Published on: September 26, 2025

629

Related Concept Videos

Responses to Heat and Cold Stress02:45

Responses to Heat and Cold Stress

Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
14.7K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.3K
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
551
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
8.8K