Exploring functional redundancy in the immunoglobulin mu heavy-chain gene enhancer.

Abstract:

:Immunoglobulin (Ig) mu 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, muE2 and muE3, 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 mu enhancer in nonlymphoid cells and defined the domains of the ETS gene required for function.

journal_name

Mol Cell Biol

authors

Dang W,Nikolajczyk BS,Sen R

doi

10.1128/mcb.18.11.6870

subject

Has Abstract

pub_date

1998-11-01 00:00:00

pages

6870-8

issue

11

eissn

0270-7306

issn

1098-5549

journal_volume

18

pub_type

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