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The SCAN domain mediates selective oligomerization.

C Schumacher¹, H Wang, C Honer

¹Novartis Institute for Biomedical Research, Summit, New Jersey 07901 and Myriad Genetics, Salt Lake City, Utah 84108, USA. schumacher@pharma.novartis.com

The Journal of Biological Chemistry

|April 5, 2000

Summary

The SCAN domain, a protein motif in zinc finger proteins, mediates protein-protein interactions. This study identifies new SCAN domain proteins, revealing its role in regulating transcription.

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Area of Science:

Molecular Biology
Protein Interactions
Transcription Factors

Background:

The SCAN (Starts Coiled-coil Associated Nucleation) domain is a conserved leucine-rich motif found in zinc finger transcription factors.
Its function was unclear, but its structure suggested a role in protein-protein interactions.

Purpose of the Study:

To investigate the function of the SCAN domain in protein associations.
To identify novel proteins interacting with the SCAN domain of ZNF202.

Main Methods:

Yeast two-hybrid screening to identify interacting proteins.
Biochemical binding assays to confirm interactions.

Main Results:

Identified ZNF191 and a novel protein, SDP1, interacting with the ZNF202 SCAN domain.

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ZNF191 represents a SCAN domain-containing zinc finger protein family.

SDP1 represents a new family encoding an isolated SCAN domain, capable of homodimerization.

Confirmed SCAN domain mediates selective hetero- and homotypic oligomerization.

Conclusions:

The SCAN domain acts as a selective oligomerization domain.
SCAN-mediated protein associations may represent a novel regulatory mechanism for transcriptional activity.