The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network
Open accessAbstract
The role of small heat-shock proteins in Escherichia coli is still enigmatic. We show here that the small heat-shock protein IbpB is a molecular chaperone that assists the refolding of denatured proteins in the presence of other chaperones. IbpB oligomers bind and stabilize heat-denatured malate dehydrogenase (MDH) and urea-denatured lactate dehydrogenase and thus prevent the irreversible aggregation of these proteins during stress. While IbpB-stabilized proteins alone do not refold spontaneously, they are specifically delivered to the DnaK/DnaJ/GrpE (KJE) chaperone system where they refold in a strict ATPase-dependent manner. Although GroEL/GroES (LS) chaperonins do not interact directly with IbpB-released proteins, LS accelerate the rate of KJE-mediated refolding of IbpB-released MDH, and to a lesser extent lactate dehydrogenase, by rapidly processing KJE-released early intermediates. Kinetic and gel-filtration analysis showed that denatured MDH preferentially transfers from IbpB to KJE, then from KJE to LS, and then forms a active enzyme. IbpB thus stabilizes aggregation-prone folding intermediates during stress and, as an integral part of a cooperative multichaperone network, is involved in the active refolding of stress-denatured proteins.
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Cites
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Cited by
Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
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Recombinant protein folding and misfolding in Escherichia coli
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Advanced genetic strategies for recombinant protein expression in Escherichia coli
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Hsp26: a temperature-regulated chaperone
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Metadata
- Authors
- Veinger, L., Diamant, S., Buchner, J., & Goloubinoff, P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-05
- Volume
- 273
- Issue
- 18
- Pages
- 11032-11037
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2150041704
- Cited by
- 353
- References
- 23
- FWCI
- 5.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Veinger, L., Diamant, S., Buchner, J., & Goloubinoff, P. (1998). The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.18.11032
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
