IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB
Authors:
- Elzbieta Ratajczak,
- Joanna Teresa Stróżecka,
- Marlena Matuszewska,
- Szymon Zietkiewicz,
- Dorota Kuczyńska-Wiśnik,
- Ewa Laskowska,
- Krzysztof Liberek
Abstract
Small heat shock proteins (sHsps) associate with aggregated proteins, changing their physical properties in such a way that chaperone mediated disaggregation becomes much more efficient. In Escherichia coli two small Hsps, IbpA and IbpB, exist. They are 48% identical at the amino acid level, yet their roles in stabilisation of protein aggregates are quite distinct. Here we analysed the biochemical properties of IbpA. We found that IbpA assembles into protofilaments which in turn form mature fibrils. Such fibrils are atypical for sHsps. Interaction of IbpA with either its cochaperone IbpB or an aggregated substrate blocks IbpA fibril formation. © 2010 Federation of European Biochemical Societies.
- Record ID
- UAM1d2b1e3ab6c443e9b3bd762c3a05a439
- Author
- Journal series
- FEBS Letters, ISSN 0014-5793
- Issue year
- 2010
- Vol
- 584
- Pages
- 2253-2257
- ASJC Classification
- ; ; ; ; ;
- DOI
- DOI:10.1016/j.febslet.2010.04.060 Opening in a new tab
- Language
- (en) English
- Score (nominal)
- 0
- Score source
- journalList
- Publication indicators
- = 12; : 2010 = 0.792; : 2010 (2 years) = 3.601 - 2010 (5 years) =3.399
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- Uniform Resource Identifier
- https://researchportal.amu.edu.pl/info/article/UAM1d2b1e3ab6c443e9b3bd762c3a05a439/
- URN
urn:amu-prod:UAM1d2b1e3ab6c443e9b3bd762c3a05a439
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or PerishOpening in a new tab system.