Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 13, Pages 13114-13121Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M412649200
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Funding
- NCI NIH HHS [CA72699] Funding Source: Medline
- NIAID NIH HHS [AI54821] Funding Source: Medline
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BCL-6 functions as a potent transcriptional repressor that binds with specificity to DNA elements bearing marked similarity to STAT recognition sequences. Previous studies have demonstrated that BCL-6 and Stat6 can both bind and regulate the I is an element of promoter that controls immunoglobulin heavy chain class switching to IgE. Examination of BCL-6(-/-) and BCL-6(-/-) Stat6(-/-) mice has demonstrated that BCL-6 is a repressor of IgE and that Stat6 is still required for the interleukin-4 (IL-4) induction of class switching to IgE in B cells lacking BCL-6. To define the mechanisms by which BCL-6 represses IL-4 function, we analyzed the role of BCL-6 in repressing the I is an element of promoter. There are three BCL-6-binding sites within this IL-4-responsive promoter. Analysis of I is an element of promoters that have mutated BCL-6-binding sites demonstrates that at least two of these sites are required for maximal BCL-6 repression of this locus. Footprinting analysis demonstrates that BCL-6 binds cooperatively to the two upstream binding sites in the I is an element of promoter. This cooperative binding requires the POZ domain of BCL-6. Furthermore, activated Stat6 molecules can displace BCL-6 from one of these binding sites. These data demonstrate that cooperative interaction between BCL-6 molecules is required for repression of the I is an element of promoter.
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