Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104
| Autor: | Daniel R. Southworth, Adam L. Yokom, Nathan M. Kendsersky, Elizabeth A. Sweeny, Korrie L. Mack, JiaBei Lin, James Shorter, Min Su, Alexandrea N. Rizo, Meredith E. Jackrel, Courtney E. Buell, Mariana P. Torrente, Stephanie N. Gates, Edward Chuang |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Conformational change Saccharomyces cerevisiae Proteins Protein domain Saccharomyces cerevisiae Random hexamer Article Substrate Specificity 03 medical and health sciences Protein Domains Promoter Regions Genetic Heat-Shock Proteins chemistry.chemical_classification Multidisciplinary biology Nucleotides Hydrolysis Cryoelectron Microscopy Caseins biology.organism_classification Transport protein Amino acid Protein Transport 030104 developmental biology Proteostasis chemistry Biochemistry Chaperone (protein) biology.protein Biophysics Tyrosine Peptides |
| Zdroj: | Science. 357:273-279 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.aan1052 |
| Popis: | Untangling aggregates one step at a time Conserved AAA+ protein complexes exploit adenosine triphosphate hydrolysis to unfold and disaggregate their substrates in response to cell stress, but exactly how they do this has been unclear. Gates et al. determined high-resolution cryo-electron microscopy structures of the Hsp104 disaggregase bound to an unfolded polypeptide substrate in its channel. The structures reveal substrate interactions and two different translocation states. Hsp104 undergoes conformational changes that drive movement along the substrate by two-amino-acid steps. These states help explain how this molecular machine can solubilize protein aggregates and amyloids. Science , this issue p. 273 |
| Databáze: | OpenAIRE |
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