Single Asparagine to Arginine Mutation Allows PerR to Switch from PerR Box to Fur Box
| Autor: | Christelle Caux-Thang, Arhamatoulaye Maïga, Ramakrishnan Sethu, Aubérie Parent, Jean-Marc Latour, Geneviève Blondin, Victor Duarte |
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| Přispěvatelé: | Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA) |
| Rok vydání: | 2014 |
| Předmět: |
DNA
Bacterial Transcription Genetic Molecular Sequence Data Virulence Bacillus subtilis Biology Arginine Biochemistry DNA sequencing 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Transcription (biology) [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] Protein Interaction Domains and Motifs Nucleotide Asparagine Gene 030304 developmental biology Genetics chemistry.chemical_classification 0303 health sciences Base Sequence integumentary system 030306 microbiology Gene Expression Regulation Bacterial General Medicine biology.organism_classification [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Repressor Proteins chemistry Mutation bacteria Molecular Medicine DNA Protein Binding |
| Zdroj: | ACS Chemical Biology ACS Chemical Biology, American Chemical Society, 2015, 10 (3), pp.682-686. ⟨10.1021/cb500783g⟩ ACS Chemical Biology, 2015, 10 (3), pp.682-686. ⟨10.1021/cb500783g⟩ |
| ISSN: | 1554-8937 1554-8929 |
| Popis: | International audience; Fur family proteins, ubiquitous in prokaryotes, play a pivotal role in microbial survival and virulence in most pathogens. Metalloregulators, such as Fur and PerR, regulate the transcription of genes connected to iron homeostasis and response to oxidative stress, respectively. In Bacillus subtilis, Fur and PerR bind with high affinity to DNA sequences differing at only two nucleotides. In addition to these differences in the PerR and Fur boxes, we identify in this study a residue located on the DNA binding motif of the Fur protein that is critical to discrimination between the two close DNA sequences. Interestingly, when this residue is introduced into PerR, it lowers the affinity of PerR for its own DNA target but confers to the protein the ability to interact strongly with the Fur DNA binding sequence. The present data show how two closely related proteins have distinct biological properties just by changing a single residue. |
| Databáze: | OpenAIRE |
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