PMID: 8986808Dec 24, 1996Paper

HMG I(Y) interferes with the DNA binding of NF-AT factors and the induction of the interleukin 4 promoter in T cells

Proceedings of the National Academy of Sciences of the United States of America
S Klein-HesslingE Serfling

Abstract

HMG I(Y) proteins bind to double-stranded A + T oligonucleotides longer than three base pairs. Such motifs form part of numerous NF-AT-binding sites of lymphokine promoters, including the interleukin 4 (IL-4) promoter. NF-AT factors share short homologous peptide sequences in their DNA-binding domain with NF-kappa B factors and bind to certain NF-kappa B sites. It has been shown that HMG I(Y) proteins enhance NF-kappa B binding to the interferon beta promoter and virus-mediated interferon beta promoter induction. We show that HMG I(Y) proteins exert an opposite effect on the DNA binding of NF-AT factors and the induction of the IL-4 promoter in T lymphocytes. Introduction of mutations into a high-affinity HMG I(Y)-binding site of the IL-4 promoter, which decreased HMG I(Y)-binding to a NF-AT-binding sequence, the Pu-bB (or P) site, distinctly increased the induction of the IL-4 promoter in Jurkat T leukemia cells. High concentrations of HMG I(Y) proteins are able to displace NF-ATp from its binding to the Pu-bB site. High HMG I(Y) concentrations are typical for Jurkat cells and peripheral blood T lymphocytes, whereas E14 T lymphoma cells and certain T helper type 2 cell clones contain relatively low HMG I(Y) concentrations. Our...Continue Reading

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Citations

Jun 19, 2001·Biochimica Et Biophysica Acta·R Reeves, L Beckerbauer
Jan 27, 1998·Immunobiology·M Li-WeberP H Krammer
Oct 30, 1998·Cellular Signalling·E S MasudaN Arai
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Nov 12, 2018·Reproduction, Fertility, and Development·Hao-Ran LiFei-Xue Li
Jan 12, 2002·The Journal of Biological Chemistry·Bin ZhouH Scott Baldwin
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