Related Experiment Video

Updated: Jun 12, 2025

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

6.2K

Characterization of the Biological Effect Mediated by Mycobacterial Kinase PknG on Protein Phosphorylation and

Shuyu Xie1,2,3, Tianqi Liu1, Luoxi Zhang4

  • 1Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.

ACS Omega
|June 9, 2025
PubMed

Insights

This study reveals how Protein Kinase G (PknG) in mycobacteria affects protein phosphorylation and lysine acetylation, impacting energy metabolism and virulence. These findings offer new targets for tuberculosis treatment.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Tuberculosis (TB) is a major global health issue.
  • Post-translational modifications (PTMs) in mycobacteria are crucial for pathogenesis and drug resistance.
  • Protein Kinase G (PknG) is a secreted kinase linked to virulence and drug resistance, but its regulatory targets are not fully understood.

Purpose of the Study:

  • To systematically investigate the proteome and phosphoproteome alterations in mycobacteria upon PknG overexpression.
  • To elucidate the regulatory role of MsPknG in mycobacterial physiology.
  • To explore the interplay between phosphorylation and other PTMs, like lysine acetylation.

Main Methods:

  • Overexpression of MsPknG in mycobacteria.
  • Quantitative proteomic and phosphoproteomic analysis.
  • Bioinformatic analysis to identify regulated proteins and phosphorylation sites.

Main Results:

  • Identified 3836 proteins and 467 phosphorylation sites regulated by MsPknG.
  • MsPknG regulates energy metabolism and binding processes.
  • Observed a reduction in lysine acetylation linked to carbon metabolism and energy pathways in PknG-overexpressing strains.

Conclusions:

  • MsPknG plays a significant role in regulating mycobacterial metabolism and virulence.
  • The study provides insights into the interplay of PTMs in mycobacteria.
  • Identified potential therapeutic targets for tuberculosis treatment.

More Related Videos

Assaying Protein Kinase Activity with Radiolabeled ATP08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

18.3K
Identification of Kinase-substrate Pairs Using High Throughput Screening11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

8.1K

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.8K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.4K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
6.2K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K