Functional domains and upstream activation properties of cloned human TATA binding protein

Michael Gregory Peterson, Naoko Tanese, Benjamin Franklin Pugh, Robert Tjian

Research output: Contribution to journalArticle

302 Citations (Scopus)

Abstract

The TATA binding protein, TFIID, plays a central role in the initiation of eukaryotic mRNA synthesis. Here, we present a human cDNA clone for this factor. Comparison of its predicted protein sequence with those from Drosophila and yeast reveals a highly conserved carboxyl-terminal 180 amino acids. By contrast, the amino-terminal region of TFIID has diverged in both sequence and length. A striking feature of the human protein is a stretch of 38 glutamine residues in the NH 2 -terminal region. Expression of human TFIID in both Escherichia coli and HeLa cells produces a protein that binds specifically to a TATA box and promotes basal transcription; the conserved COOH-terminal portion of the protein is sufficient for both of these activities. Recombinant TFIID forms a stable complex on a TATA box either alone or in combination with either of the general transcription factors, TFTIA or TFIIB. Full-length recombinant TFiID is able to support Sp1 activated transcription in a TFIID-depleted nuclear extract, while a deletion of the NH 2 -terminal half of the protein is not. These results indicate the importance of the NH 2 -terminal region for upstream activation functions and suggest that additional factors (co-activators) are required for mediating interactions with specific regulators.

Original languageEnglish (US)
Pages (from-to)1625-1630
Number of pages6
JournalScience
Volume248
Issue number4963
DOIs
StatePublished - Jan 1 1990

Fingerprint

Transcription Factor TFIID
TATA-Box Binding Protein
TATA Box
Proteins
Transcription Factor TFIIB
General Transcription Factors
Glutamine
HeLa Cells
Drosophila
Complementary DNA
Clone Cells
Yeasts
Escherichia coli
Amino Acids
Messenger RNA

All Science Journal Classification (ASJC) codes

  • General

Cite this

Peterson, Michael Gregory ; Tanese, Naoko ; Pugh, Benjamin Franklin ; Tjian, Robert. / Functional domains and upstream activation properties of cloned human TATA binding protein. In: Science. 1990 ; Vol. 248, No. 4963. pp. 1625-1630.
@article{055429d15945448aa12ece8fe5015170,
title = "Functional domains and upstream activation properties of cloned human TATA binding protein",
abstract = "The TATA binding protein, TFIID, plays a central role in the initiation of eukaryotic mRNA synthesis. Here, we present a human cDNA clone for this factor. Comparison of its predicted protein sequence with those from Drosophila and yeast reveals a highly conserved carboxyl-terminal 180 amino acids. By contrast, the amino-terminal region of TFIID has diverged in both sequence and length. A striking feature of the human protein is a stretch of 38 glutamine residues in the NH 2 -terminal region. Expression of human TFIID in both Escherichia coli and HeLa cells produces a protein that binds specifically to a TATA box and promotes basal transcription; the conserved COOH-terminal portion of the protein is sufficient for both of these activities. Recombinant TFIID forms a stable complex on a TATA box either alone or in combination with either of the general transcription factors, TFTIA or TFIIB. Full-length recombinant TFiID is able to support Sp1 activated transcription in a TFIID-depleted nuclear extract, while a deletion of the NH 2 -terminal half of the protein is not. These results indicate the importance of the NH 2 -terminal region for upstream activation functions and suggest that additional factors (co-activators) are required for mediating interactions with specific regulators.",
author = "Peterson, {Michael Gregory} and Naoko Tanese and Pugh, {Benjamin Franklin} and Robert Tjian",
year = "1990",
month = "1",
day = "1",
doi = "10.1126/science.2363050",
language = "English (US)",
volume = "248",
pages = "1625--1630",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "4963",

}

Functional domains and upstream activation properties of cloned human TATA binding protein. / Peterson, Michael Gregory; Tanese, Naoko; Pugh, Benjamin Franklin; Tjian, Robert.

In: Science, Vol. 248, No. 4963, 01.01.1990, p. 1625-1630.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Functional domains and upstream activation properties of cloned human TATA binding protein

AU - Peterson, Michael Gregory

AU - Tanese, Naoko

AU - Pugh, Benjamin Franklin

AU - Tjian, Robert

PY - 1990/1/1

Y1 - 1990/1/1

N2 - The TATA binding protein, TFIID, plays a central role in the initiation of eukaryotic mRNA synthesis. Here, we present a human cDNA clone for this factor. Comparison of its predicted protein sequence with those from Drosophila and yeast reveals a highly conserved carboxyl-terminal 180 amino acids. By contrast, the amino-terminal region of TFIID has diverged in both sequence and length. A striking feature of the human protein is a stretch of 38 glutamine residues in the NH 2 -terminal region. Expression of human TFIID in both Escherichia coli and HeLa cells produces a protein that binds specifically to a TATA box and promotes basal transcription; the conserved COOH-terminal portion of the protein is sufficient for both of these activities. Recombinant TFIID forms a stable complex on a TATA box either alone or in combination with either of the general transcription factors, TFTIA or TFIIB. Full-length recombinant TFiID is able to support Sp1 activated transcription in a TFIID-depleted nuclear extract, while a deletion of the NH 2 -terminal half of the protein is not. These results indicate the importance of the NH 2 -terminal region for upstream activation functions and suggest that additional factors (co-activators) are required for mediating interactions with specific regulators.

AB - The TATA binding protein, TFIID, plays a central role in the initiation of eukaryotic mRNA synthesis. Here, we present a human cDNA clone for this factor. Comparison of its predicted protein sequence with those from Drosophila and yeast reveals a highly conserved carboxyl-terminal 180 amino acids. By contrast, the amino-terminal region of TFIID has diverged in both sequence and length. A striking feature of the human protein is a stretch of 38 glutamine residues in the NH 2 -terminal region. Expression of human TFIID in both Escherichia coli and HeLa cells produces a protein that binds specifically to a TATA box and promotes basal transcription; the conserved COOH-terminal portion of the protein is sufficient for both of these activities. Recombinant TFIID forms a stable complex on a TATA box either alone or in combination with either of the general transcription factors, TFTIA or TFIIB. Full-length recombinant TFiID is able to support Sp1 activated transcription in a TFIID-depleted nuclear extract, while a deletion of the NH 2 -terminal half of the protein is not. These results indicate the importance of the NH 2 -terminal region for upstream activation functions and suggest that additional factors (co-activators) are required for mediating interactions with specific regulators.

UR - http://www.scopus.com/inward/record.url?scp=0025375345&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025375345&partnerID=8YFLogxK

U2 - 10.1126/science.2363050

DO - 10.1126/science.2363050

M3 - Article

C2 - 2363050

AN - SCOPUS:0025375345

VL - 248

SP - 1625

EP - 1630

JO - Science

JF - Science

SN - 0036-8075

IS - 4963

ER -