The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
Two Families of Chaperonin: Physiology and Mechanism
Abstract
Chaperonins are large ring assemblies that assist protein folding to the native state by binding nonnative proteins in their central cavities and then, upon binding ATP, release the substrate protein into a now-encapsulated cavity to fold productively. Two families of such components have been identified: type I in mitochondria, chloroplasts, and the bacterial cytosol, which rely on a detachable “lid” structure for encapsulation, and type II in archaea and the eukaryotic cytosol, which contain a built-in protrusion structure. We discuss here a number of issues under current study. What is the range of substrates acted on by the two classes of chaperonin, in particular by GroEL in the bacterial cytoplasm and CCT in the eukaryotic cytosol, and are all these substrates subject to encapsulation? What are the determinants for substrate binding by the type II chaperonins? And is the encapsulated chaperonin cavity a passive container that prevents aggregation, or could it be playing an active role in polypeptide folding?
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2 retracted
Siegers, K., Bölter, B., Schwarz, J. P., Böttcher, U. M. K., Guha, S., & Hartl, F. U. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601964 · Cited by 104
RetractedTRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
Siegers, K., Bölter, B., Schwarz, J. P., Böttcher, U. M. K., Guha, S., & Hartl, F. U. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg483 · Cited by 92
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Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A.-C., Bösche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A.-M., Cruciat, C.-M., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,759
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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From Levinthal to pathways to funnels
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The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
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Self-citationThe crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
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Self-citation
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Yam, A. Y., Xia, Y., Lin, H.-T. J., Burlingame, A., Gerstein, M., & Frydman, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1515 · Cited by 420
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Metadata
- Authors
- Horwich, A. L., Fenton, W. A., Chapman, E., & Farr, G. W.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2007-11-01
- Volume
- 23
- Issue
- 1
- Pages
- 115-145
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2121963790
- Cited by
- 422
- References
- 78
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- closed
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