論文 - 詳細
| RRC ID | 76054 |
|---|---|
| 著者 | Schmauder L, Absmeier E, Bepperling A, Barkovits K, Marcus K, Richter K. |
| タイトル | Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90. |
| ジャーナル | Sci Rep |
| Abstract |
The molecular chaperones Hsc70 and Hsp90 are required for proteostasis control and specific folding of client proteins in eukaryotic and prokaryotic organisms. Especially in eukaryotes these ATP-driven molecular chaperones are interacting with cofactors that specify the client spectrum and coordinate the ATPase cycles. Here we find that a Hsc70-cofactor of the Hsp40 family from nematodes, DNJ-13, directly interacts with the kinase-specific Hsp90-cofactor CDC-37. The interaction is specific for DNJ-13, while DNJ-12 another DnaJ-like protein of C. elegans, does not bind to CDC-37 in a similar manner. Analytical ultracentrifugation is employed to show that one CDC-37 molecule binds to a dimeric DNJ-13 protein with low micromolar affinity. We perform cross-linking studies with mass spectrometry to identify the interaction site and obtain specific cross-links connecting the N-terminal J-domain of DNJ-13 with the N-terminal domain of CDC-37. Further AUC experiments reveal that both, the N-terminal part of CDC-37 and the C-terminal domain of CDC-37, are required for efficient interaction. Furthermore, the presence of DNJ-13 strengthens the complex formation between CDC-37 and HSP-90 and modulates the nucleotide-dependent effects. These findings on the interaction between Hsp40 proteins and Hsp90-cofactors provide evidence for a more intricate interaction between the two chaperone systems during client processing. |
| 巻・号 | 11(1) |
| ページ | 21346 |
| 公開日 | 2021-11-1 |
| DOI | 10.1038/s41598-021-00885-4 |
| PII | 10.1038/s41598-021-00885-4 |
| PMID | 34725424 |
| PMC | PMC8560915 |
| MeSH | Animals Caenorhabditis elegans / chemistry Caenorhabditis elegans / metabolism* Caenorhabditis elegans Proteins / chemistry Caenorhabditis elegans Proteins / metabolism* Cell Cycle Proteins / chemistry Cell Cycle Proteins / metabolism* HSP40 Heat-Shock Proteins / chemistry HSP40 Heat-Shock Proteins / metabolism* HSP90 Heat-Shock Proteins / chemistry HSP90 Heat-Shock Proteins / metabolism* Models, Molecular Protein Binding Protein Folding Protein Interaction Maps |
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