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PMID: 2187178 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterisation of the DNA binding domain of the yeast RAP1 protein.

Nucleic acids research ·Vol. 18 ·No. 9 ·1990-05-11 ·Pages 2617-23

Henry YA, Chambers A, Tsang JS, Kingsman AJ, Kingsman SM

Abstract

The 827 amino acid yeast RAP1 protein interacts with DNA to regulate gene expression at numerous unrelated loci in the yeast genome. By a combination of amino, carboxy and internal deletions, we have defined an internal 235 amino acid fragment of the yeast RAP1 protein that can bind efficiently to the RAP1 binding site of the PGK Upstream Activation Sequence (UAS). This domain spans residues 361 to 596 of the full length protein and lacks any homology to the DNA binding 'zinc finger' or 'helix-turn-helix' structural motifs. All the RAP1 binding sites we have tested bind domain 361-596, arguing that RAP1 binds all its chromosomal sites via this domain. The domain could not be further reduced in size suggesting that it represents the minimal functional DNA binding domain. The relevance of potential regions of secondary structure within the minimal binding domain is discussed.

MeSH Terms
Base Sequence DNA, Fungal/metabolism DNA-Binding Proteins/metabolism Electrophoresis, Polyacrylamide Gel Fungal Proteins/metabolism Molecular Sequence Data Protein Conformation Regulatory Sequences, Nucleic Acid Restriction Mapping Saccharomyces cerevisiae/genetics Transcription Factors
Chemicals
DNA, Fungal DNA-Binding Proteins Fungal Proteins Transcription Factors
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Henry Y A
Department of Biochemistry, Oxford University, UK.
Chambers A
Tsang J S
Kingsman A J
Kingsman S M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/18.9.2617
Published
1990-05-11
Pages
2617-23
Language
English
Region
England
NLM ID
0411011
PMCID
PMC330744
Subset
IM
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1093/nar/18.9.2617 PMC Full Text View journal details
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