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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Unique structural modulation of a non-native substrate by cochaperone DnaJ.

Satyam Tiwari1, Vignesh Kumar, Gopal Gunanathan Jayaraj

  • 1Proteomics and Structural Biology Unit, CSIR-Institute of Genomics and Integrative Biology, South Campus, Mathura Road, Delhi 110020, India.

Biochemistry
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Summary

Bacterial DnaJ protein, a cochaperone, can individually bind and alter non-native proteins. This unique structural modulation by DnaJ suggests a novel unfolding activity, potentially aiding protein folding.

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Area of Science:

  • Molecular Biology
  • Protein Folding
  • Chaperone Proteins

Background:

  • The bacterial DnaJ protein is a well-established cochaperone for DnaK.
  • Its role as an individual chaperone, independent of DnaK, remains largely unexplored.

Purpose of the Study:

  • To investigate the chaperone activity of DnaJ acting alone.
  • To characterize the interaction between DnaJ and non-native substrate proteins.
  • To elucidate the structural changes induced by DnaJ binding.

Main Methods:

  • Binding assays to determine the dissociation constant of DnaJ to a model non-native substrate.
  • Structural analysis to compare the effects of DnaJ alone versus the DnaK-DnaJ complex.
  • Mutational analysis of DnaJ domains (zinc binding motif, C-terminal substrate binding domain).

Main Results:

  • DnaJ binds a model non-native substrate with high affinity (low nanomolar dissociation constant).
  • DnaJ induces structural modulation of the non-native substrate, distinct from DnaK-DnaJ complex effects.
  • The zinc binding motif and C-terminal substrate binding domain of DnaJ are essential and sufficient for substrate binding and structural modulation.
  • The observed structural modulation suggests a unique unfolding activity by DnaJ.

Conclusions:

  • Bacterial DnaJ possesses intrinsic chaperone activity, capable of binding and altering non-native proteins independently.
  • DnaJ's ability to modulate substrate structure may involve a novel unfolding mechanism.
  • This DnaJ-mediated structural alteration is hypothesized to resolve kinetic traps in protein folding intermediates.