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Histone Modification

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

Histone Modification

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

Covalently Linked Protein Regulators

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 RER

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 Glycosylation

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...

Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

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Related Experiment Video

Updated: May 14, 2026

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

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

Published on: February 27, 2020

Deciphering post-translational modification codes.

Adam P Lothrop¹, Matthew P Torres, Stephen M Fuchs

¹Department of Biology, Tufts University, 200 Boston Ave. Suite 4700, Medford, MA 02155, USA.

|February 14, 2013

Summary

This summary is machine-generated.

Combinatorial post-translational modifications (PTMs) create diverse protein species. Understanding these PTM patterns is crucial for deciphering distinct biological outcomes and advancing protein science.

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Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Post-translational modifications (PTMs) are fundamental to protein function, occurring on nearly all proteins.
Proteins can be modified by multiple enzymes on various amino acid side chains, generating a vast array of protein forms.
The biological consequences of these complex PTM combinations are not yet fully understood.

Purpose of the Study:

To highlight examples of combinatorial PTMs in proteins.
To describe technological advancements enabling the study of PTM patterns.
To explore how PTM combinations may encode specific biological functions.

Main Methods:

Literature review of existing studies on combinatorial PTMs.
Analysis of recent technological developments in PTM detection and characterization.
Case study examples illustrating the impact of PTM combinations.

Main Results:

Multiple proteins exhibit complex patterns of combinatorial PTMs.
Emerging technologies are significantly enhancing the ability to map and interpret these PTM patterns.
Specific PTM combinations are linked to distinct biological activities.

Conclusions:

The combinatorial nature of PTMs generates significant protein diversity.
Advancements in technology are key to understanding the functional implications of PTM codes.
Deciphering PTM patterns offers new insights into cellular regulation and function.