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

Heidi Rommelaere, Myriam De Neve UGent, Ronald Melki, Joël Vandekerckhove and Christophe Ampe UGent (1999) BIOCHEMISTRY. 38(11). p.3246-3257
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
T-COMPLEX POLYPEPTIDE-1, CYTOPLASMIC CHAPERONIN, MOLECULAR CHAPERONE, BETA-TUBULIN, STRUCTURAL CHARACTERIZATION, SUBSTRATE-BINDING, GROEL, ACTIN, SUBUNITS, DOMAIN
journal title
BIOCHEMISTRY
Biochemistry
volume
38
issue
11
pages
3246 - 3257
Web of Science type
Article
Web of Science id
000079510600004
ISSN
0006-2960
DOI
10.1021/bi9815905
language
English
UGent publication?
yes
classification
A1
id
173516
handle
http://hdl.handle.net/1854/LU-173516
date created
2004-01-14 13:40:00
date last changed
2018-01-04 13:01:04
@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},
}

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.