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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.
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Related Experiment Video

Updated: Mar 26, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Analysis of Protein Sumoylation.

Kevin D Sarge¹

¹Department of Biochemistry, University of Kentucky, Lexington, Kentucky.

Current Protocols in Protein Science

|February 3, 2016

Summary

Identifying new sumoylated proteins expands our understanding of cellular processes. This study details two assays to detect protein sumoylation and pinpoint modification sites, aiding functional analysis.

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Sumoylation, the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to lysine residues, is a crucial post-translational modification.
This process regulates diverse cellular functions by altering the properties of target proteins.

Purpose of the Study:

To describe reliable methods for identifying sumoylated proteins.
To facilitate the discovery of novel sumoylated proteins and expand the understanding of sumoylation's role in cell function.

Main Methods:

Immunoprecipitation followed by SUMO immunoblotting to detect sumoylated proteins.
In vitro sumoylation assays with subsequent SDS-PAGE analysis to identify modified proteins.
Site-directed mutagenesis (lysine-to-arginine substitutions) to pinpoint specific sumoylation sites.

Keywords:

SUMO-1 SUMO-2 SUMO-3 Ubc9 post-translational modification sumoylation

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Main Results:

Two distinct and effective assays for detecting protein sumoylation are presented.
The methods allow for the identification of sumoylated proteins and the precise localization of sumoylation sites.
These techniques enable the subsequent functional analysis of sumoylation on specific proteins.

Conclusions:

The described assays provide valuable tools for researchers studying sumoylation.
Expanding the catalog of sumoylated proteins will deepen insights into cellular regulation.
Understanding sumoylation site-specific effects is key to elucidating protein function.