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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.
RNA Editing02:23

RNA Editing

RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect 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.
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.
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Is there a code embedded in proteins that is based on post-translational modifications?

Robert J Sims1, Danny Reinberg

  • 1Constellation Pharmaceuticals, 148 Sidney Street, Cambridge, Massachusetts 02139, USA. roberts@constellationpharma.com

Nature Reviews. Molecular Cell Biology
|September 12, 2008
PubMed
Summary
This summary is machine-generated.

Covalent post-translational modifications (PTMs) on proteins, including histones, act as recognition sites for effectors. This leads to complex interactions and downstream events, similar to other regulatory pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Covalent post-translational modifications (PTMs) expand protein functionality.
  • The 'histone code' hypothesis initially focused on chromatin biology.
  • The relevance of PTMs is now recognized for non-histone proteins.

Purpose of the Study:

  • To analyze the role of protein covalent modifications beyond a simple 'code'.
  • To understand how PTMs create interaction surfaces for downstream signaling.
  • To explore the parallels between PTM-mediated regulation and other cellular cascades.

Main Methods:

  • Comprehensive analysis of existing literature and data on protein modifications.
  • Comparative studies of histone and non-histone protein modification patterns.
  • Investigating effector recognition mechanisms for modified proteins.

Main Results:

  • Protein covalent modifications, including histones, function as recognition platforms rather than a strict code.
  • These modifications facilitate intricate protein-protein interactions.
  • PTM-driven interactions initiate downstream cellular events, mirroring transcription and signaling pathways.

Conclusions:

  • Covalent PTMs provide regulatory surfaces recognized by specific effectors.
  • This recognition mechanism drives complex biological outcomes.
  • PTM-based regulation is a fundamental principle in cellular signaling and gene expression.