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PMID: 8171010 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Transcriptional activation by CTF proteins is mediated by a bipartite low-proline domain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 9 ·1994-04-26 ·Pages 3901-5

Altmann H, Wendler W, Winnacker EL

Abstract

Members of the CCAAT-binding transcription factor (CTF) family of proteins stimulate the initiation of adenovirus DNA replication and act as transcriptional activators. To investigate the mechanisms underlying CTF-mediated transactivation patterns, we expressed several natural CTF variants in Saccharomyces cerevisiae and determined their transactivating activities in enzymatic assays. CTF7, which lacks the entire proline-rich region previously thought to mediate transcriptional activation by CTF proteins, enhances transcription to a greater degree than full-length CTF1, which contains the putative activation domain. CTF2, which contains a partially deleted proline-rich activation region, does not stimulate transcription at all. These findings indicate that the proline-rich region of CTF proteins is not essential for transcriptional activation in yeast. Our studies also suggest a bipartite two-domain structure of CTF-type transcriptional activation domains.

Related Genes
CTF1 CTF2 CTF7 NF1
MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Base Sequence CCAAT-Enhancer-Binding Proteins DNA Primers/chemistry DNA-Binding Proteins/chemistry,genetics Gene Expression Regulation, Fungal In Vitro Techniques Molecular Sequence Data Neurofibromin 1 Nuclear Proteins/chemistry,genetics Proline Proteins/chemistry RNA, Messenger/genetics Recombinant Proteins Saccharomyces cerevisiae/genetics Structure-Activity Relationship Swine Transcription, Genetic Transcriptional Activation
Chemicals
CCAAT-Enhancer-Binding Proteins DNA Primers DNA-Binding Proteins Neurofibromin 1 Nuclear Proteins Proteins RNA, Messenger Recombinant Proteins Proline
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Altmann H
Institut für Biochemie der Ludwig-Maximilians-Universität, Martinsried, Germany.
Wendler W
Winnacker E L
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32 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.9.3901
Published
1994-04-26
Pages
3901-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC43690
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.91.9.3901 PMC Full Text View journal details
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