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Tagging and Fusion Proteins

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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Ultrasmall Chemogenetic Tags with Group-Transfer Ligands.

Vedagopuram Sreekanth¹, Shaimaa H Sindi¹, Santosh K Chaudhary¹

¹Chemical Biology and Therapeutics Science, Broad Institute of MIT and Harvard, Cambridge, MA, 02142, USA.

Angewandte Chemie (International Ed. in English)

|September 27, 2025

Summary

This summary is machine-generated.

Researchers developed ultrasmall chemogenetic tags (mgTag and cTag) for studying proteins. These novel tags are the smallest available, enabling new possibilities in biotechnology and medicine.

Keywords:

C1 domain Chemogenetic tags Induced proximity KRAS signaling Molecular glue

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Published on: January 17, 2019

Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

Chemogenetic tags are crucial for studying protein function when small-molecule ligands are unavailable.
Existing tags are often too large, hindering their application with certain proteins of interest (POIs).

Purpose of the Study:

To develop and characterize novel, ultrasmall chemogenetic tags for broader POI applications.
To demonstrate the utility of these tags in maintaining protein function and inducing proximity.

Main Methods:

Engineered two ultrasmall chemogenetic tags: mgTag (36 aa) and cTag (50 aa).
Utilized transferase-type reactivity for ligand attachment.
Assessed tag impact on KRAS(G12D) signaling pathway.
Investigated proximity induction between Abelson kinase (ABL) and BRD4 using tagged proteins.

Main Results:

mgTag and cTag are the smallest reported chemogenetic tags.
Fusion of mgTag or cTag to KRAS(G12D) did not disrupt its growth-signaling pathway, unlike larger tags.
Group-transfer of a BRD4 binder to tagged ABL induced proximity and phosphorylation of BRD4.
Reduced phosphorylation was observed when transferase-type reactivity was deleted.

Conclusions:

Ultrasmall chemogenetic tags (mgTag, cTag) overcome limitations of larger tags.
These tags enable functional studies and proximity-induced signaling.
The group-transfer mechanism offers an effective strategy for designing proximity-inducing chimeras.
The tags have broad potential applications in basic science, biotechnology, and medicine.