Publications
1991
Mueller C G, Nordheim A
A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation Journal Article
In: The EMBO journal, vol. 10, no. 13, pp. 4219–4229, 1991, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Amino Acid Sequence, Base Sequence, DNA, DNA-Binding Proteins, Fungal, Fungal Proteins, Humans, Minichromosome Maintenance 1 Protein, Molecular Sequence Data, Nuclear Proteins, Nucleic Acid, Plasmids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Serum Response Factor, Team-Mueller, Transcription Factors
@article{mueller_protein_1991,
title = {A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation},
author = {C G Mueller and A Nordheim},
issn = {0261-4189},
year = {1991},
date = {1991-12-01},
journal = {The EMBO journal},
volume = {10},
number = {13},
pages = {4219--4229},
abstract = {MCM1 and SRF bind to the same DNA sequence and form ternary complexes with STE12 and p62TCF, respectively. We show that in gel retardation assays, MCM1 recruits both ternary complex factors whereas SRF interacts only with p62TCF. A protein domain of 90 amino acids, shared by MCM1 and SRF, was found to be sufficient for ternary complex formation. The domain is also required for dimerization and DNA binding. Similar regions are found in other proteins, such as ARG80, Deficiens and Agamous. ARG80 and Agamous exhibit similar DNA binding specificities but do not interact with either STE12 or p62TCF. By exchanging three residues of ARG80 with those of corresponding positions in SRF (residues 198, 200 and 203), the ARG80 protein acquires the ability to recruit p62TCF into a ternary complex. Likewise, the substitution of four SRF amino acids by MCM1-derived residues (amino acids 73, 75, 77 and 78) confers on SRF the ability to interact with STE12. Thus, we have identified specific amino acids in MCM1 and SRF that are critical for ternary complex formation and which map to equivalent positions within the shared domains. Therefore, the structural basis for specific protein-protein interaction appears to be conserved in evolution between a class of transcription factors.},
keywords = {Amino Acid Sequence, Base Sequence, DNA, DNA-Binding Proteins, Fungal, Fungal Proteins, Humans, Minichromosome Maintenance 1 Protein, Molecular Sequence Data, Nuclear Proteins, Nucleic Acid, Plasmids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Serum Response Factor, Team-Mueller, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
1990
Schröter H, Mueller C G, Meese K, Nordheim A
Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element Journal Article
In: The EMBO journal, vol. 9, no. 4, pp. 1123–1130, 1990, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors
@article{schroter_synergism_1990,
title = {Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element},
author = {H Schröter and C G Mueller and K Meese and A Nordheim},
issn = {0261-4189},
year = {1990},
date = {1990-04-01},
journal = {The EMBO journal},
volume = {9},
number = {4},
pages = {1123--1130},
abstract = {Transcriptional regulation of the c-fos proto-oncogene requires the serum response element (SRE) which is complexed by a multi-protein assembly observed both in vitro and in vivo. Two protein factors, p67SRF and p62TCF (previously called p62), are required to interact with the SRE for efficient induction of c-fos by serum. By quantitative band shift electrophoresis we measure at least a 50-fold increase in SRE affinity for p67SRF/p62TCF over p67SRF alone. Stoichiometrically we determine that the ternary complex with p62TCF involves p67SRF in dimeric form. We demonstrate that p67SRF is a glycosylated nuclear transcription factor carrying terminal N-acetylglucosamine (GlcNAc) as a post-translational modification. A proteolytic limit digestion product, approximately 13 kd in size, was generated from the p67SRF-SRE complex. This p67SRF-core domain binds SRE, can dimerize with p67SRF and is still able to form a ternary complex with p62TCF. Therefore, three functional activities can be ascribed to this small p67SRF-core domain: specific DNA binding, dimerization and interaction with p62TCF. We demonstrate that these functions map within the p67SRF core fragment containing the region between amino acids 93 and 222.},
keywords = {Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}