Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB

Lawrence D. Kerr; Lynn J. Ransone; Penny Wamsley; Mark J. Schmitt; Thomas G. Boyer; Qiang Zhou; Arnold J. Berk; Inder M. Verma

doi:10.1038/365412a0

Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB

Lawrence D. Kerr, Lynn J. Ransone, Penny Wamsley, Mark J. Schmitt, Thomas G. Boyer, Qiang Zhou, Arnold J. Berk, Inder M. Verma

Research output: Contribution to journal › Article › peer-review

129 Scopus citations

Abstract

The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the κB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fail to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between κB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.

Original language	English (US)
Pages (from-to)	412-419
Number of pages	8
Journal	Nature
Volume	365
Issue number	6445
DOIs	https://doi.org/10.1038/365412a0
State	Published - Jan 1 1993
Externally published	Yes

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Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB. / Kerr, Lawrence D.; Ransone, Lynn J.; Wamsley, Penny; Schmitt, Mark J.; Boyer, Thomas G.; Zhou, Qiang; Berk, Arnold J.; Verma, Inder M.

In: Nature, Vol. 365, No. 6445, 01.01.1993, p. 412-419.

Research output: Contribution to journal › Article › peer-review

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abstract = "The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the κB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fail to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between κB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.",

author = "Kerr, {Lawrence D.} and Ransone, {Lynn J.} and Penny Wamsley and Schmitt, {Mark J.} and Boyer, {Thomas G.} and Qiang Zhou and Berk, {Arnold J.} and Verma, {Inder M.}",

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AU - Kerr, Lawrence D.

AU - Ransone, Lynn J.

AU - Wamsley, Penny

AU - Schmitt, Mark J.

AU - Boyer, Thomas G.

AU - Zhou, Qiang

AU - Berk, Arnold J.

AU - Verma, Inder M.

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N2 - The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the κB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fail to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between κB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.

AB - The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the κB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fail to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between κB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.

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Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB

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