TFIIA regulates TBP and TFIID dimers

Robert A. Coleman, Andrew K P Taggart, Sandeep Burma, John J. Chicca, B. Franklin Pugh

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.

Original languageEnglish (US)
Pages (from-to)451-457
Number of pages7
JournalMolecular Cell
Volume4
Issue number3
DOIs
StatePublished - Sep 1999
Externally publishedYes

Fingerprint

Transcription Factor TFIIA
Transcription Factor TFIID
TATA-Box Binding Protein
DNA
Protein Multimerization
Gene Expression
Dimerization

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Coleman, R. A., Taggart, A. K. P., Burma, S., Chicca, J. J., & Pugh, B. F. (1999). TFIIA regulates TBP and TFIID dimers. Molecular Cell, 4(3), 451-457. https://doi.org/10.1016/S1097-2765(00)80453-0

TFIIA regulates TBP and TFIID dimers. / Coleman, Robert A.; Taggart, Andrew K P; Burma, Sandeep; Chicca, John J.; Pugh, B. Franklin.

In: Molecular Cell, Vol. 4, No. 3, 09.1999, p. 451-457.

Research output: Contribution to journalArticle

Coleman, RA, Taggart, AKP, Burma, S, Chicca, JJ & Pugh, BF 1999, 'TFIIA regulates TBP and TFIID dimers', Molecular Cell, vol. 4, no. 3, pp. 451-457. https://doi.org/10.1016/S1097-2765(00)80453-0
Coleman RA, Taggart AKP, Burma S, Chicca JJ, Pugh BF. TFIIA regulates TBP and TFIID dimers. Molecular Cell. 1999 Sep;4(3):451-457. https://doi.org/10.1016/S1097-2765(00)80453-0
Coleman, Robert A. ; Taggart, Andrew K P ; Burma, Sandeep ; Chicca, John J. ; Pugh, B. Franklin. / TFIIA regulates TBP and TFIID dimers. In: Molecular Cell. 1999 ; Vol. 4, No. 3. pp. 451-457.
@article{17f347020a5546a8ae51a9fc8ed486ee,
title = "TFIIA regulates TBP and TFIID dimers",
abstract = "Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.",
author = "Coleman, {Robert A.} and Taggart, {Andrew K P} and Sandeep Burma and Chicca, {John J.} and Pugh, {B. Franklin}",
year = "1999",
month = "9",
doi = "10.1016/S1097-2765(00)80453-0",
language = "English (US)",
volume = "4",
pages = "451--457",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - TFIIA regulates TBP and TFIID dimers

AU - Coleman, Robert A.

AU - Taggart, Andrew K P

AU - Burma, Sandeep

AU - Chicca, John J.

AU - Pugh, B. Franklin

PY - 1999/9

Y1 - 1999/9

N2 - Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.

AB - Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.

UR - http://www.scopus.com/inward/record.url?scp=0033197553&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033197553&partnerID=8YFLogxK

U2 - 10.1016/S1097-2765(00)80453-0

DO - 10.1016/S1097-2765(00)80453-0

M3 - Article

VL - 4

SP - 451

EP - 457

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 3

ER -