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 Previous Article

Molecular and Cellular Biology, November 1998, p. 6870-6878, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Exploring Functional Redundancy in the Immunoglobulin µ Heavy-Chain Gene Enhancer

Wei Dang, Barbara S. Nikolajczyk, and Ranjan Sen*

Rosenstiel Research Center and Departments of Biology and Biochemistry, Brandeis University, Waltham, Massachusetts 02254

Received 1 May 1998/Returned for modification 9 June 1998/Accepted 22 July 1998

Immunoglobulin (Ig) µ heavy-chain gene enhancer activity is mediated by multiple DNA binding proteins. Mutations of several protein binding sites in the enhancer do not affect enhancer activity significantly. This feature, termed redundancy, is thought to be due to functional compensation of the mutated sites by other elements within the enhancer. In this study, we identified the elements that make the basic helix-loop-helix (bHLH) protein binding sites, µE2 and µE3, redundant. The major compensatory element is a binding site for interferon regulatory factors (IRFs) and not one of several other bHLH protein binding sites. These studies also provide the first evidence for a role of IRF proteins in Ig heavy-chain gene expression. In addition, we reconstituted the activity of a monomeric µ enhancer in nonlymphoid cells and defined the domains of the ETS gene required for function.

* Corresponding author. Mailing address: Rosenstiel Research Center, Brandeis University, 415 South St., Waltham, MA 02254. Phone: (781) 736-2455. Fax: (781) 736-2405. E-mail: sen{at}binah.cc.brandeis.edu.

Molecular and Cellular Biology, November 1998, p. 6870-6878, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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