The yeast GAL11 protein binds to the transcription factor IIE through GAL11 regions essential for its in vivo function

Hiroshi Sakurai, Young Joon Kim, Tomoko Ohishi, Roger D. Kornberg, Toshio Fukasawa

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The GAL11 gene encodes an auxiliary transcription factor required for full expression of many genes in yeast. The GAL11-encoded protein (Gal 11 p) has recently been shown to copurify with the holoenzyme of RNA polymerase II. Here we report that Gal11p stimulates basal transcription in a reconstituted transcription system composed of recombinant or highly purified transcription factors, TFIIB, TFIIE, TFIIF, TFIIH, and TATA box-binding protein and core RNA polymerase II. We further demonstrate that each of the two domains of Gal11p essential for in vivo function respectively participates in the binding to the small and large subunits of TFIIE. The largest subunit of RNA polymerase 11 was coprecipitated by anti-hemagglutinin epitope antibody from crude extract of GAL11 wild type yeast expressing hemagglutinintagged small subunit of TFIIE. Such a coprecipitation of the RNA polymerase subunit was seen but in a greatly reduced amount, if extract was prepared from gal11 null yeast. In light of these findings, we suggest that Gal11p stimulates promoter activity by enhancing an association of TFIIE with the preinitiation complex in the cell.

Original languageEnglish
Pages (from-to)9488-9492
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number18
DOIs
Publication statusPublished - 1996 Sep 3

Fingerprint

Fungal Proteins
RNA Polymerase II
Yeasts
DNA-Directed RNA Polymerases
Transcription Factor TFIIB
TATA-Box Binding Protein
Holoenzymes
Hemagglutinins
Complex Mixtures
Epitopes
Transcription Factors
Gene Expression
transcription factor TFIIE
Antibodies
Genes
Proteins

All Science Journal Classification (ASJC) codes

  • General

Cite this

@article{21cd0a1081954da6bfb4b61a2d56d713,
title = "The yeast GAL11 protein binds to the transcription factor IIE through GAL11 regions essential for its in vivo function",
abstract = "The GAL11 gene encodes an auxiliary transcription factor required for full expression of many genes in yeast. The GAL11-encoded protein (Gal 11 p) has recently been shown to copurify with the holoenzyme of RNA polymerase II. Here we report that Gal11p stimulates basal transcription in a reconstituted transcription system composed of recombinant or highly purified transcription factors, TFIIB, TFIIE, TFIIF, TFIIH, and TATA box-binding protein and core RNA polymerase II. We further demonstrate that each of the two domains of Gal11p essential for in vivo function respectively participates in the binding to the small and large subunits of TFIIE. The largest subunit of RNA polymerase 11 was coprecipitated by anti-hemagglutinin epitope antibody from crude extract of GAL11 wild type yeast expressing hemagglutinintagged small subunit of TFIIE. Such a coprecipitation of the RNA polymerase subunit was seen but in a greatly reduced amount, if extract was prepared from gal11 null yeast. In light of these findings, we suggest that Gal11p stimulates promoter activity by enhancing an association of TFIIE with the preinitiation complex in the cell.",
author = "Hiroshi Sakurai and Kim, {Young Joon} and Tomoko Ohishi and Kornberg, {Roger D.} and Toshio Fukasawa",
year = "1996",
month = "9",
day = "3",
doi = "10.1073/pnas.93.18.9488",
language = "English",
volume = "93",
pages = "9488--9492",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "18",

}

The yeast GAL11 protein binds to the transcription factor IIE through GAL11 regions essential for its in vivo function. / Sakurai, Hiroshi; Kim, Young Joon; Ohishi, Tomoko; Kornberg, Roger D.; Fukasawa, Toshio.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, No. 18, 03.09.1996, p. 9488-9492.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The yeast GAL11 protein binds to the transcription factor IIE through GAL11 regions essential for its in vivo function

AU - Sakurai, Hiroshi

AU - Kim, Young Joon

AU - Ohishi, Tomoko

AU - Kornberg, Roger D.

AU - Fukasawa, Toshio

PY - 1996/9/3

Y1 - 1996/9/3

N2 - The GAL11 gene encodes an auxiliary transcription factor required for full expression of many genes in yeast. The GAL11-encoded protein (Gal 11 p) has recently been shown to copurify with the holoenzyme of RNA polymerase II. Here we report that Gal11p stimulates basal transcription in a reconstituted transcription system composed of recombinant or highly purified transcription factors, TFIIB, TFIIE, TFIIF, TFIIH, and TATA box-binding protein and core RNA polymerase II. We further demonstrate that each of the two domains of Gal11p essential for in vivo function respectively participates in the binding to the small and large subunits of TFIIE. The largest subunit of RNA polymerase 11 was coprecipitated by anti-hemagglutinin epitope antibody from crude extract of GAL11 wild type yeast expressing hemagglutinintagged small subunit of TFIIE. Such a coprecipitation of the RNA polymerase subunit was seen but in a greatly reduced amount, if extract was prepared from gal11 null yeast. In light of these findings, we suggest that Gal11p stimulates promoter activity by enhancing an association of TFIIE with the preinitiation complex in the cell.

AB - The GAL11 gene encodes an auxiliary transcription factor required for full expression of many genes in yeast. The GAL11-encoded protein (Gal 11 p) has recently been shown to copurify with the holoenzyme of RNA polymerase II. Here we report that Gal11p stimulates basal transcription in a reconstituted transcription system composed of recombinant or highly purified transcription factors, TFIIB, TFIIE, TFIIF, TFIIH, and TATA box-binding protein and core RNA polymerase II. We further demonstrate that each of the two domains of Gal11p essential for in vivo function respectively participates in the binding to the small and large subunits of TFIIE. The largest subunit of RNA polymerase 11 was coprecipitated by anti-hemagglutinin epitope antibody from crude extract of GAL11 wild type yeast expressing hemagglutinintagged small subunit of TFIIE. Such a coprecipitation of the RNA polymerase subunit was seen but in a greatly reduced amount, if extract was prepared from gal11 null yeast. In light of these findings, we suggest that Gal11p stimulates promoter activity by enhancing an association of TFIIE with the preinitiation complex in the cell.

UR - http://www.scopus.com/inward/record.url?scp=0029821144&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029821144&partnerID=8YFLogxK

U2 - 10.1073/pnas.93.18.9488

DO - 10.1073/pnas.93.18.9488

M3 - Article

C2 - 8790357

AN - SCOPUS:0029821144

VL - 93

SP - 9488

EP - 9492

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 18

ER -