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Protein-Protein Interactions: Oxidative Bacterial Two Hybrid.

Authors
  • Pellegri, Callypso1
  • Bouveret, Emmanuelle2
  • Houot, Laetitia3
  • 1 Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR7255, Institut de Microbiologie de la Méditerranée, Aix-Marseille Univ - CNRS, Marseille, France. , (France)
  • 2 Institut Pasteur, Department of Microbiology, Unit Stress, Adaptation and Metabolism in enterobacteria, Université Paris Cité, UMR CNRS 6047, Paris, France. , (France)
  • 3 Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR7255, Institut de Microbiologie de la Méditerranée, Aix-Marseille Univ - CNRS, Marseille, France. [email protected]. , (France)
Type
Published Article
Journal
Methods in molecular biology
Publisher
Clifton, N.J. : Humana Press
Publication Date
Jan 01, 2024
Volume
2715
Pages
225–233
Identifiers
DOI: 10.1007/978-1-0716-3445-5_14
PMID: 37930531
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Protein-protein interaction studies are essential to understand how proteins organize themselves into interaction networks and thus influence cellular processes. Protein binding specificity depends on the correct three-dimensional folding of the polypeptide sequences. One of the forces involved in the structuring and stability of proteins is the formation of disulfide bonds. These covalent bonds are formed posttranscriptionally by the oxidation of a pair of cysteine residues and can serve structural, catalytic, or signaling roles. Here, we describe an engineered E. coli adenylate cyclase mutant strain with an oxidative cytoplasm that promotes correct folding of proteins with disulfide bonds. This genetic background expands the set of host strains suitable for studying protein-protein interactions in vivo by the adenylate cyclase two-hybrid approach. © 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

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