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PMID: 8029001 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The upstream activator CTF/NF1 and RNA polymerase II share a common element involved in transcriptional activation.

Nucleic acids research ·Vol. 22 ·No. 11 ·1994-06-11 ·Pages 1966-73

Xiao H, Lis JT, Xiao H, Greenblatt J, Friesen JD

Abstract

The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II consists of tandem repeats of a heptapeptide with the consensus YSPTSPS. It has been shown that the heptapeptide repeat interacts directly with the general transcription factor TFIID. We report here that the CTD activates transcription when fused to the DNA-binding domain of GAL4. More importantly, we find that the proline-rich transcriptional activation domain of the CCAAT-box-binding factor CTF/NF1 contains a sequence with striking similarity to the heptapeptide repeats of the CTD. We show that this CTD-like motif is essential for the transcriptional activator function of the proline-rich domain of CTF/NF1. Deletion of and point mutations in this CTD-like motif abolish the transcriptional activator function of the proline-rich domain, while natural CTD repeats from RNA polymerase II are fully functional in place of the CTD-like motif. We further show that the proline-rich activation domain of CTF/NF1 interacts directly with the TATA-box-binding protein (TBP), and that a mutation in the CTD-like motif that abolishes transcriptional activation reduces the affinity of the proline-rich domain for TBP. These results demonstrate that a class of proline-rich activator proteins and RNA polymerase II possess a common structural and functional component which can interact with the same target in the general transcription machinery. We discuss the implications of these results for the mechanisms of transcriptional activation in eucaryotes.

MeSH Terms
Amino Acid Sequence Base Sequence Chromosomal Proteins, Non-Histone Consensus Sequence DNA, Fungal DNA-Binding Proteins/metabolism Fungal Proteins/chemistry,metabolism Molecular Sequence Data Proline/metabolism RNA Polymerase II/chemistry,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins TATA Box TATA-Box Binding Protein Transcription Factors/metabolism Transcriptional Activation Transformation, Genetic
Chemicals
CHL1 protein, S cerevisiae Chromosomal Proteins, Non-Histone DNA, Fungal DNA-Binding Proteins Fungal Proteins Saccharomyces cerevisiae Proteins TATA-Box Binding Protein Transcription Factors Proline RNA Polymerase II
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Xiao H
Department of Genetics, Hospital for Sick Children, Toronto, Ontario, Canada.
Lis J T
Xiao H
Greenblatt J
Friesen J D
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1994-06-11
Pages
1966-73
Language
English
Region
England
NLM ID
0411011
PMCID
PMC308108
Subset
IM
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