The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
| Autor: | C Ampe, J Vandekerckhove, Heidi Rommelaere, Ronald Melki, M De Neve |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Reticulocytes genetic structures Chaperonins Molecular Sequence Data macromolecular substances Biology Biochemistry Binding Competitive Chaperonin Mice Cytosol Tubulin Native state Animals Actin-binding protein Amino Acid Sequence Peptide sequence Actin Sequence Deletion Binding Sites Cell-Free System Molecular Mimicry Cooperative binding Chaperonin 60 Molecular biology GroEL eye diseases Actins Peptide Fragments Cell biology biology.protein Mutagenesis Site-Directed sense organs Rabbits Chaperonin Containing TCP-1 |
| Zdroj: | Biochemistry. 38(11) |
| ISSN: | 0006-2960 |
| Popis: | The nonhomologous proteins actin and alpha- and beta-tubulin need the assistance of the cytosolic chaperonin containing TCP-1 (CCT) to reach their correct native state, and their folding requires a transient binary complex formation with CCT. We show that separate or combined deletion of three delineated hydrophobic sequences in actin disturbs the interaction with CCT. These sites are situated between residues 125-179, 244-285, and 340-375. Also, alpha- and beta-tubulin contain at least one recognition region, and intriguingly, it has a similar distribution of hydrophobic residues as region 244-285 in actin. Internal deletion of the sites in actin favor a model for cooperative binding of target proteins to CCT. Peptide mimetics, representing the binding regions, inhibit target polypeptide binding to CCT, suggesting that actin and tubulin contact similar CCT subunits. In addition, we show that actin recognition by class II chaperonins is different from that by class I. |
| Databáze: | OpenAIRE |
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