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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.
Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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.
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...

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Related Experiment Video

Updated: May 7, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

What pathogens have taught us about posttranslational modifications.

Dor Salomon1, Kim Orth

  • 1Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA.

Cell Host & Microbe
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

Pathogen research has illuminated how microbes manipulate host cells. This study details how pathogens advance our knowledge of crucial protein modifications like phosphorylation, N-linked protein modification (NMPylation), and ubiquitylation in cellular processes and infection.

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Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

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Last Updated: May 7, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Area of Science:

  • Microbiology
  • Molecular Biology
  • Cell Biology

Background:

  • Pathogens employ diverse strategies to subvert host cellular functions for their own propagation.
  • Understanding host-pathogen interactions reveals fundamental cellular mechanisms, including signaling pathways and protein regulation.

Purpose of the Study:

  • To explore the significant contributions of pathogen research to the understanding of key posttranslational modifications.
  • To highlight the roles of phosphorylation, N-linked protein modification (NMPylation), and ubiquitylation in host-pathogen dynamics.

Main Methods:

  • Review of existing literature on pathogen-mediated manipulation of host processes.
  • Analysis of how pathogen studies have advanced the discovery and characterization of posttranslational modifications.
  • Examination of the interplay between technological advancements and the study of protein modifications in infection.

Main Results:

  • Pathogen research has been instrumental in uncovering the functional significance of posttranslational modifications.
  • Specific examples illustrate how pathogens exploit phosphorylation, NMPylation, and ubiquitylation to their advantage.
  • The study of pathogens has driven the development of novel techniques for identifying and analyzing protein modifications.

Conclusions:

  • Pathogens serve as powerful tools for dissecting fundamental cellular processes, including protein modification.
  • Continued investigation into host-pathogen interactions promises further insights into cell biology and disease mechanisms.
  • Advancements in research technologies have been crucial for unraveling the complexities of protein modifications in the context of infection.