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Molecular and Cellular Biology, December 1999, p. 8526-8535, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain

Amy J. Williams, Stephen C. Blacklow, and Tucker Collins*

Department of Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02115

Received 14 July 1999/Returned for modification 8 August 1999/Accepted 27 August 1999

A number of Cys2His2 zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be alpha -helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.

* Corresponding author. Mailing address: Brigham and Women's Hospital, Vascular Research Division, 221 Longwood Ave., Boston, MA 02115. Phone: (617) 732-5990. Fax: (617) 278-6990. E-mail: tcollins{at}bustoff.bwh.harvard.edu.

Molecular and Cellular Biology, December 1999, p. 8526-8535, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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