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Related Concept Videos

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.
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.
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...
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...

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Related Experiment Video

Updated: May 27, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Thiol-based posttranslational modifications in parasites.

Esther Jortzik1, Lihui Wang, Katja Becker

  • 1Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.

Antioxidants & Redox Signaling
|November 17, 2011
PubMed
Summary
This summary is machine-generated.

Cysteine posttranslational modifications (PTMs) regulate parasitic protein function and are key to parasite survival. Understanding these modifications in vivo is crucial for developing new anti-parasitic strategies.

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

Published on: January 8, 2018

Related Experiment Videos

Last Updated: May 27, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

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

Area of Science:

  • Biochemistry
  • Parasitology
  • Molecular Biology

Background:

  • Human parasites undergo significant changes during their life cycles, influenced by protein modifications.
  • Cysteine posttranslational modifications (PTMs) are vital for parasite adaptation, regulating processes like signal transduction, protein trafficking, and host cell interaction.
  • Key cysteine PTMs in parasites include S-glutathionylation, S-nitrosylation, palmitoylation, and prenylation.

Purpose of the Study:

  • To review the occurrence and mechanisms of cysteine modifications in human parasites.
  • To highlight the importance of cysteine PTMs in parasite biology and disease.
  • To identify future research directions for understanding redox signaling in parasites.

Main Methods:

  • This review synthesizes existing literature on cysteine modifications in parasites.
  • Focuses on mechanisms and roles in cellular events.
  • Highlights the current reliance on in vitro studies.

Main Results:

  • Cysteine residues are critical for protein structure, function, and redox reactions.
  • Covalent PTMs of cysteine residues mediate redox regulation and signaling, impacting protein stability, function, and localization.
  • In human parasites, cysteine PTMs are involved in signal transduction, redox regulation, protein trafficking, and host cell invasion/egress.

Conclusions:

  • Cysteine PTMs are crucial for the survival and virulence of human parasites.
  • Current research predominantly relies on in vitro experiments.
  • Investigating in vivo regulation of cysteine modifications is essential for understanding parasite development and redox signaling, paving the way for novel therapeutic targets.