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The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins

(1999) BIOCHEMISTRY. 38(11). p.3246-3257
Author
Organization
Abstract
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.
Keywords
T-COMPLEX POLYPEPTIDE-1, CYTOPLASMIC CHAPERONIN, MOLECULAR CHAPERONE, BETA-TUBULIN, STRUCTURAL CHARACTERIZATION, SUBSTRATE-BINDING, GROEL, ACTIN, SUBUNITS, DOMAIN

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Chicago
Rommelaere, Heidi, Myriam De Neve, Ronald Melki, Joël Vandekerckhove, and Christophe Ampe. 1999. “The Cytosolic Class II Chaperonin CCT Recognizes Delineated Hydrophobic Sequences in Its Target Proteins.” Biochemistry 38 (11): 3246–3257.
APA
Rommelaere, H., De Neve, M., Melki, R., Vandekerckhove, J., & Ampe, C. (1999). The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. BIOCHEMISTRY, 38(11), 3246–3257.
Vancouver
1.
Rommelaere H, De Neve M, Melki R, Vandekerckhove J, Ampe C. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. BIOCHEMISTRY. 1999;38(11):3246–57.
MLA
Rommelaere, Heidi, Myriam De Neve, Ronald Melki, et al. “The Cytosolic Class II Chaperonin CCT Recognizes Delineated Hydrophobic Sequences in Its Target Proteins.” BIOCHEMISTRY 38.11 (1999): 3246–3257. Print.
@article{173516,
  abstract     = {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.},
  author       = {Rommelaere, Heidi and De Neve, Myriam and Melki, Ronald and Vandekerckhove, Jo{\"e}l and Ampe, Christophe},
  issn         = {0006-2960},
  journal      = {BIOCHEMISTRY},
  keyword      = {T-COMPLEX POLYPEPTIDE-1,CYTOPLASMIC CHAPERONIN,MOLECULAR CHAPERONE,BETA-TUBULIN,STRUCTURAL CHARACTERIZATION,SUBSTRATE-BINDING,GROEL,ACTIN,SUBUNITS,DOMAIN},
  language     = {eng},
  number       = {11},
  pages        = {3246--3257},
  title        = {The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins},
  url          = {http://dx.doi.org/10.1021/bi9815905},
  volume       = {38},
  year         = {1999},
}

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