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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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...
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Protein Kinases and Phosphatases02:54

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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...
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Covalently Linked Protein Regulators02:04

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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.
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The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Phosphorylation regulates mycobacterial proteasome.

Tripti Anandan1, Jaeil Han, Heather Baun

  • 1Department of Biological Science, Wayne State University, Detroit, MI, 48202, USA.

Journal of Microbiology (Seoul, Korea)
|September 17, 2014
PubMed
Summary

Mycobacterium tuberculosis proteasome activity is regulated by phosphorylation. Kinase PknB enhances proteasome degradation, while PknA modulates proteasome assembly, aiding survival against host immunity and oxidative stress.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The Mycobacterium tuberculosis proteasome is crucial for evading host immune responses.
  • Mechanisms controlling proteasome activity in M. tuberculosis are not well understood.

Purpose of the Study:

  • To investigate the role of protein phosphorylation in regulating M. tuberculosis proteasome function.
  • To elucidate how proteasome regulation contributes to mycobacterial survival under stress.

Main Methods:

  • Phosphorylation analysis of proteasome subunits (PrcA, pre-PrcB) by kinases (PknB, PknA).
  • Assessing the impact of phosphorylation on proteasome proteolytic activity and substrate degradation (Ino1).
  • Evaluating changes in proteasome complex formation and mycobacterial resistance to oxidative stress (H2O2, RNIs).

Main Results:

  • PknB sequentially phosphorylates PrcA at T84, T202, and T178, enhancing proteasome-mediated Ino1 degradation.
  • PknA phosphorylation of pre-PrcB and PrcA reduces proteasome complex assembly.
  • This PknA-mediated effect increases resistance to hydrogen peroxide (H2O2) and alters resistance to reactive nitrogen intermediates (RNIs).

Conclusions:

  • Phosphorylation by PknB modulates the proteolytic activity of the M. tuberculosis proteasome.
  • Phosphorylation by PknA influences proteasome complex formation, contributing to mycobacterial survival under oxidative stress.
  • These regulatory mechanisms are key to M. tuberculosis pathogenesis and persistence.