ArticleMolecular and cellular biology2002
Swapping functional specificity of a MADS box protein: residues required for Arg80 regulation of arginine metabolism.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- The other giant: functional significance and divergence of Type I MADS-box genes in the evolution of land plants.Journal of experimental botany · 2026Review
- Isolation and characterization of Saccharomyces cerevisiae mutants with ornithine accumulation for value-added craft beer brewing.Journal of industrial microbiology & biotechnology · 2026Article
- Gene loss and cis-regulatory novelty shaped core histone gene evolution in the apiculate yeast Hanseniaspora uvarum.Genetics · 2024Article
- The MADS-box genesFrontiers in plant science · 2024Article
- Effect and mechanism of signal peptide and maltose on recombinant type III collagen production in Pichia pastoris.Applied microbiology and biotechnology · 2023Article
- Analysis of Key Genes Responsible for Low Urea Production inFrontiers in microbiology · 2022Article
- Exploration and characterization of hypoxia-inducible endogenous promoters in Aspergillus niger.Applied microbiology and biotechnology · 2021Article
- Gene expression profile indicates involvement of NO in Camellia sinensis pollen tube growth at low temperature.BMC genomics · 2016Article
- Following gene duplication, paralog interference constrains transcriptional circuit evolution.Science (New York, N.Y.) · 2013Article
- From elements to modules: regulatory evolution in Ascomycota fungi.Current opinion in genetics & development · 2009Review
- Connecting protein structure with predictions of regulatory sites.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Identifying cooperative transcriptional regulations using protein-protein interactions.Nucleic acids research · 2005Article
- Recruitment of the ArgR/Mcm1p repressor is stimulated by the activator Gcn4p: a self-checking activation mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Identifying cooperativity among transcription factors controlling the cell cycle in yeast.Nucleic acids research · 2003Article
- The essential transcription factor Reb1p interacts with the CLB2 UAS outside of the G2/M control region.Nucleic acids research · 2003Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Arg80 and Mcm1, two members of the MADS box family of DNA-binding proteins, regulate the metabolism of arginine in association with Arg81, the arginine sensor. In spite of the high degree of sequence conservation between the MADS box domains of the Arg80 and Mcm1 proteins (56 of 81 amino acids), these domains are not interchangeable. To determine which amino acids define the specificity of Arg80, we swapped the amino acids in each secondary-structure element of the Arg80 MADS box domain with the corresponding amino acids of Mcm1 and assayed the ability of these chimeras to regulate arginine-metabolic genes in place of the wild-type Arg80. Also performed was the converse experiment in which each variant residue in the Mcm1 MADS box domain was swapped with the corresponding residue of Arg80 in the context of an Arg80-Mcm1 fusion protein. We show that multiple regions of Arg80 are important for its function. Interestingly, the residues which have important roles in determining the specificity of Arg80 are not those which could contact the DNA but are residues that are likely to be involved in protein interactions. Many of these residues are clustered on one side of the protein, which could serve as an interface for interaction with Arg81 or Mcm1. This interface is distinct from the region used by the Mcm1 and human serum response factor MADS box proteins to interact with their cofactors. It is possible that this alternative interface is used by other MADS box proteins to interact with their cofactors.
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