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A Conserved Acidic Amino Acid Mediates the Interaction between Modulators and Co-Chaperones in Enterobacteria
- Source :
- Journal of Molecular Biology. 411:313-320
- Publication Year :
- 2011
- Publisher :
- Elsevier BV, 2011.
-
Abstract
- Hsp40-like co-chaperones are ubiquitous enzymes that stimulate the protein refolding activity of Hsp70 family chaperones. They are widespread in prokaryotic and eukaryotic systems. In bacteria, the best characterized co-chaperone is the Escherichia coli DnaJ protein. Many γ-proteobacteria encode a functional homologue of DnaJ, known as CbpA, which is expressed in response to starvation and environmental stress. The activity of CbpA is regulated by the “modulator” protein CbpM. Here, we have used a combination of genetics and biochemistry to identify the co-chaperone contact determinant of CbpM. We show that the nature of the interaction is conserved in enterobacteria.
- Subjects :
- Amino Acids, Acidic
DNAJ Protein
medicine.disease_cause
Protein–protein interaction
Bacterial Proteins
Enterobacteriaceae
Structural Biology
Protein Interaction Mapping
medicine
DNAJB1
Molecular Biology
Escherichia coli
Conserved Sequence
Phylogeny
chemistry.chemical_classification
Sequence Homology, Amino Acid
biology
Escherichia coli Proteins
HSP40 Heat-Shock Proteins
biology.organism_classification
Amino acid
Enzyme
Biochemistry
chemistry
DNAJA2
Carrier Proteins
Bacteria
Protein Binding
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 411
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....507f42d912bc2c29b3b0bd178f4aa32e