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Related Experiment Video

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A Simple Flight Mill for the Study of Tethered Flight in Insects

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Published on: December 10, 2015

Structure and function of a human TAFII250 double bromodomain module.

R H Jacobson¹, A G Ladurner, D S King

¹Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720-3204, USA.

Science (New York, N.Y.)

|May 29, 2000

Summary

The TFIID complex recognizes acetylated histone H4 tails via its TAFII250 subunit. This bromodomain interaction suggests a mechanism for targeting transcription factors to chromatin-bound promoters.

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Area of Science:

Molecular Biology
Chromatin Biology
Gene Transcription

Background:

Transcription Factor II D (TFIID) is crucial for initiating gene transcription.
Mechanisms by which TFIID recognizes nucleosome-bound promoters in vivo remain largely unknown.

Purpose of the Study:

To investigate how TFIID interacts with nucleosomal DNA to initiate transcription.
To elucidate the role of the TAFII250 subunit in promoter recognition.

Main Methods:

X-ray crystallography to determine the structure of TAFII250 bromodomains.
Biochemical assays to assess binding affinity to acetylated histone peptides.

Main Results:

TAFII250, the largest TFIID subunit, possesses tandem bromodomain modules.
These bromodomains selectively bind to multiply acetylated histone H4 peptides.
The crystal structure reveals a unique architecture suited for recognizing diacetylated histone H4 tails.

Conclusions:

TFIID utilizes TAFII250 bromodomains for specific recognition of acetylated histone H4.
This interaction provides a potential mechanism for targeting TFIID to chromatin-bound promoters.
TFIID may play a direct role in chromatin recognition during transcription initiation.