IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB.
FEBS Lett
; 584(11): 2253-7, 2010 Jun 03.
Article
em En
| MEDLINE
| ID: mdl-20433838
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Corpos de Inclusão
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Chaperonas Moleculares
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Proteínas de Escherichia coli
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Escherichia coli
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Proteínas de Choque Térmico
Limite:
Animals
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article