Behind closed gates – chaperones and charged residues determine protein fate
| Autor: | Koopman, Margreet B., Rüdiger, Stefan G.D., Sub Cellular Protein Chemistry, Cellular Protein Chemistry |
|---|---|
| Přispěvatelé: | Sub Cellular Protein Chemistry, Cellular Protein Chemistry |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0303 health sciences
General Immunology and Microbiology biology Biochemistry Genetics and Molecular Biology(all) General Neuroscience Neuroscience(all) Computational biology Biochemistry General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Chaperone (protein) Immunology and Microbiology(all) Taverne biology.protein Protein folding Molecular Biology 030217 neurology & neurosurgery 030304 developmental biology Genetics and Molecular Biology(all) |
| Zdroj: | EMBO Journal, 39(11), 1. Nature Publishing Group |
| ISSN: | 0261-4189 |
| Popis: | Charged residues flanking aggregation-prone regions play a role in protein folding and prevention of aggregation. In this issue of The EMBO Journal, Houben et al exploit the role of such charged gatekeepers in aggregation suppression and find that negative charges are more effective than positive ones. Strikingly, the prominent Hsp70 chaperone has a strong preference for the less effective, basic gate keepers. This implies co-adaptation of chaperone specificity and composition of protein sequences in evolution. |
| Databáze: | OpenAIRE |
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