scholarly journals Localization of Subunits of Transcription Factors IIE and IIF Immediately Upstream of the Transcriptional Initiation Site of the Adenovirus Major Late Promoter

1996 ◽  
Vol 271 (15) ◽  
pp. 8517-8520 ◽  
Author(s):  
François Robert ◽  
Diane Forget ◽  
Joyce Li ◽  
Jack Greenblatt ◽  
Benoit Coulombe
Keyword(s):  
Transcription Factors ◽  
Initiation Site ◽  
Late Promoter ◽  
Transcriptional Initiation ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter ◽  
Transcriptional Initiation Site

scholarly journals Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II.

1991 ◽  
Vol 11 (3) ◽  
pp. 1195-1206 ◽  
Author(s):  
E Bengal ◽  
O Flores ◽  
A Krauskopf ◽  
D Reinberg ◽  
Y Aloni
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Gel Filtration ◽  
Late Promoter ◽  
Elongation Complex ◽  
Cell Extracts ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter ◽  
Transcription Complexes

We have used a recently developed system that allows the isolation of complexes competent for RNA polymerase II elongation (E. Bengal, A. Goldring, and Y. Aloni, J. Biol. Chem. 264:18926-18932, 1989). Pulse-labeled transcription complexes were formed at the adenovirus major late promoter with use of HeLa cell extracts. Elongation-competent complexes were purified from most of the proteins present in the extract, as well as from loosely bound elongation factors, by high-salt gel filtration chromatography. We found that under these conditions the nascent RNA was displaced from the DNA during elongation. These column-purified complexes were used to analyze the activities of different transcription factors during elongation by RNA polymerase II. We found that transcription factor IIS (TFIIS), TFIIF, and TFIIX affected the efficiency of elongation through the adenovirus major late promoter attenuation site and a synthetic attenuation site composed of eight T residues. These factors have distinct activities that depend on whether they are added before RNA polymerase has reached the attenuation site or at the time when the polymerase is pausing at the attenuation site. TFIIS was found to have antiattenuation activity, while TFIIF and TFIIX stimulated the rate of elongation. In comparison with TFIIF, TFIIS is loosely bound to the elongation complex. We also found that the activities of the factors are dependent on the nature of the attenuator. These results indicate that at least three factors play a major role during elongation by RNA polymerase II.

scholarly journals The adenovirus major late promoter TATA box and initiation site are both necessary for transcriptionin vitro

1984 ◽  
Vol 12 (19) ◽  
pp. 7423-7433 ◽  
Author(s):  
Michael F. Concino ◽  
Richard F. Lee ◽  
James P. Merryweather ◽  
Roberto Weinmann
Keyword(s):  
Initiation Site ◽  
Tata Box ◽  
Late Promoter ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter

Factors involved in specific transcription by mammalian RNA polymerase II: role of transcription factors IIA, IID, and IIB during formation of a transcription-competent complex

1990 ◽  
Vol 10 (12) ◽  
pp. 6335-6347
Author(s):  
E Maldonado ◽  
I Ha ◽  
P Cortes ◽  
L Weis ◽  
D Reinberg
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase Ii ◽  
Transcriptional Start Site ◽  
Late Promoter ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter ◽  
Tata Motif ◽  
Single Polypeptide ◽  
The Stability

Human transcription factor TFIID, the TATA-binding protein, was partially purified to a form capable of associating stably with the TATA motif of the adenovirus major late promoter. Binding of the human and yeast TFIID to the TATA motif was stimulated by TFIIA. TFIIA is an integral part of a complex capable of binding other transcription factors. A complex formed with human TFIID and TFIIA (DA complex) was specifically recognized by TFIIB. We found that TFIIB activity was contained in a single polypeptide of 32 kDa and that this polypeptide participated in transcription and was capable of binding to the DA complex to form the DAB complex. Formation of the DAB complex required TFIIA, TFIID, and sequences downstream of the transcriptional start site; however, the DA complex could be formed on an oligonucleotide containing only the adenovirus major late promoter TATA motif. Using anti-TFIIB antibodies and reagents that affect the stability of a transcription-competent complex, we found that yeast and human TFIID yielded DAB complexes with different stabilities.

scholarly journals Factors involved in specific transcription by mammalian RNA polymerase II: role of transcription factors IIA, IID, and IIB during formation of a transcription-competent complex.

1990 ◽  
Vol 10 (12) ◽  
pp. 6335-6347 ◽  
Author(s):  
E Maldonado ◽  
I Ha ◽  
P Cortes ◽  
L Weis ◽  
D Reinberg
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase Ii ◽  
Transcriptional Start Site ◽  
Late Promoter ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter ◽  
Tata Motif ◽  
Single Polypeptide ◽  
The Stability

Human transcription factor TFIID, the TATA-binding protein, was partially purified to a form capable of associating stably with the TATA motif of the adenovirus major late promoter. Binding of the human and yeast TFIID to the TATA motif was stimulated by TFIIA. TFIIA is an integral part of a complex capable of binding other transcription factors. A complex formed with human TFIID and TFIIA (DA complex) was specifically recognized by TFIIB. We found that TFIIB activity was contained in a single polypeptide of 32 kDa and that this polypeptide participated in transcription and was capable of binding to the DA complex to form the DAB complex. Formation of the DAB complex required TFIIA, TFIID, and sequences downstream of the transcriptional start site; however, the DA complex could be formed on an oligonucleotide containing only the adenovirus major late promoter TATA motif. Using anti-TFIIB antibodies and reagents that affect the stability of a transcription-competent complex, we found that yeast and human TFIID yielded DAB complexes with different stabilities.

Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II

1991 ◽  
Vol 11 (3) ◽  
pp. 1195-1206 ◽  
Author(s):  
E Bengal ◽  
O Flores ◽  
A Krauskopf ◽  
D Reinberg ◽  
Y Aloni
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Gel Filtration ◽  
Late Promoter ◽  
Elongation Complex ◽  
Cell Extracts ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter ◽  
Transcription Complexes

We have used a recently developed system that allows the isolation of complexes competent for RNA polymerase II elongation (E. Bengal, A. Goldring, and Y. Aloni, J. Biol. Chem. 264:18926-18932, 1989). Pulse-labeled transcription complexes were formed at the adenovirus major late promoter with use of HeLa cell extracts. Elongation-competent complexes were purified from most of the proteins present in the extract, as well as from loosely bound elongation factors, by high-salt gel filtration chromatography. We found that under these conditions the nascent RNA was displaced from the DNA during elongation. These column-purified complexes were used to analyze the activities of different transcription factors during elongation by RNA polymerase II. We found that transcription factor IIS (TFIIS), TFIIF, and TFIIX affected the efficiency of elongation through the adenovirus major late promoter attenuation site and a synthetic attenuation site composed of eight T residues. These factors have distinct activities that depend on whether they are added before RNA polymerase has reached the attenuation site or at the time when the polymerase is pausing at the attenuation site. TFIIS was found to have antiattenuation activity, while TFIIF and TFIIX stimulated the rate of elongation. In comparison with TFIIF, TFIIS is loosely bound to the elongation complex. We also found that the activities of the factors are dependent on the nature of the attenuator. These results indicate that at least three factors play a major role during elongation by RNA polymerase II.

Spacing requirements for simultaneous recognition of the adenovirus major late promoter TATAAAAG box and initiator element

2005 ◽  
Vol 435 (2) ◽  
pp. 347-362 ◽  
Author(s):  
Delin Ren ◽  
Yuri A. Nedialkov ◽  
Fang Li ◽  
Dianpeng Xu ◽  
Stephan Reimers ◽  
...  
Keyword(s):  
Late Promoter ◽  
Adenovirus Major Late Promoter ◽  
Initiator Element ◽  
Major Late Promoter

Downstream sequences affect transcription initiation from the adenovirus major late promoter

1986 ◽  
Vol 6 (7) ◽  
pp. 2684-2694 ◽  
Author(s):  
S L Mansour ◽  
T Grodzicker ◽  
R Tjian
Keyword(s):  
Transcription Initiation ◽  
Simian Virus 40 ◽  
T Antigen ◽  
Control Element ◽  
Coding Region ◽  
Late Promoter ◽  
Sv40 T Antigen ◽  
Transient Expression Assay ◽  
Adenovirus Major Late Promoter ◽  
Major Late Promoter

We analyzed a set of adenovirus-simian virus 40 (SV40) hybrids in which the SV40 T antigen coding sequences are inserted downstream from the adenovirus major late promoter within the first, second, and third segments of the tripartite leader. In infected cells, these viruses give rise to a matched set of hybrid SV40 mRNAs that differ only in the number of tripartite leader segments attached to the complete SV40 T antigen coding region. We found that the number of tripartite leader segments present at the 5' end of the hybrid SV40 mRNAs had little effect on the efficiency of T antigen translation. Surprisingly, insertion of SV40 sequences within the first leader segment, at +33 relative to the start of transcription, significantly reduced the frequency of transcription initiation from the major late promoter. The 3' boundary of this downstream transcriptional control element was mapped between +33 and +190 by showing that insertion of SV40 sequences within the intron after the first leader segment at +190 had very little effect on transcription initiation from the late promoter. A transient expression assay was used to show that the effect of downstream sequences on transcription initiation from the major late promoter is dependent on a trans-acting factor encoded or induced by adenovirus.

Sign in / Sign up

Export Citation Format

Share Document