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Related Concept Videos

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.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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...
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...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...

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Related Experiment Video

Updated: May 10, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Pyruvylation: a new post-translational modification mechanism.

Wanqian Guo1, Wusheng Xiao2

  • 1Department of Toxicology, State Key Laboratory of Natural and Biomimetic Drugs, School of Public Health, Peking University, Beijing, China.

Trends in Endocrinology and Metabolism: TEM
|May 8, 2026
PubMed
Summary

Researchers discovered pyruvylation, a new metabolite-controlled post-translational modification (PTM), suppresses antiviral immunity. This finding reveals pyruvylation as a potential target for novel antiviral therapies.

Keywords:
post-translational modificationpyruvatepyruvylationsignaling metabolite

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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Related Experiment Videos

Last Updated: May 10, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Post-translational modifications (PTMs) regulate protein function and cellular processes.
  • Metabolite-derived PTMs represent a critical layer of cellular regulation.
  • Type I interferon signaling is crucial for antiviral defense.

Purpose of the Study:

  • To identify novel PTMs involved in regulating immune responses.
  • To investigate the role of metabolites in controlling PTMs.
  • To explore new therapeutic strategies against viral infections.

Main Methods:

  • Proteomic analysis to identify novel PTMs.
  • Biochemical assays to characterize enzyme activity and substrate modification.
  • Cellular assays to assess the impact on interferon signaling and antiviral activity.

Main Results:

  • Pyruvylation, a modification by pyruvate, was identified as a novel PTM.
  • Pyruvylation of signal transducer and activator of transcription 1 (STAT1) was demonstrated.
  • Pyruvylation of STAT1 suppresses type I interferon signaling and antiviral immunity.

Conclusions:

  • Pyruvylation is a previously unrecognized PTM that negatively regulates antiviral immunity.
  • Metabolite-mediated PTMs, like pyruvylation, offer a new mechanism for controlling cellular processes.
  • Targeting pyruvylation presents a promising strategy for developing novel antiviral therapeutics.