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  Coupling of oligomerization and nucleotide binding in the AAA+ chaperone ClpB

Werbeck, N. D., Zeymer, C., Kellner, J., & Reinstein, J. (2011). Coupling of oligomerization and nucleotide binding in the AAA+ chaperone ClpB. Biochemistry, 50(5), 899-909. doi:10.1021/bi1018286.

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Genre: Zeitschriftenartikel
Alternativer Titel : Coupling of oligomerization and nucleotide binding in the AAA+ chaperone ClpB

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http://pubs.acs.org/doi/pdfplus/10.1021/bi1018286 (beliebiger Volltext)
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 Urheber:
Werbeck, Nicolas D.1, Autor           
Zeymer, Cathleen1, Autor           
Kellner, Julian1, Autor           
Reinstein, Jochen1, Autor           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: Members of the family of ATPases associated with various cellular activities (AAA+) typically form homohexameric ring complexes and are able to remodel their substrates, such as misfolded proteins or protein−protein complexes, in an ATP−driven process. The molecular mechanism by which ATP hydrolysis is coordinated within the multimeric complex and the energy is converted into molecular motions, however, is poorly understood. This is partly due to the fact that the oligomers formed by AAA+ proteins represent a highly complex system and analysis depends on simplification and prior knowledge. Here, we present nucleotide binding and oligomer assembly kinetics of the AAA+ protein ClpB, a molecular chaperone that is able to disaggregate protein aggregates in concert with the DnaK chaperone system. ClpB bears two AAA+ domains (NBD1 and NBD2) on one subunit and forms homohexameric ring complexes. In order to dissect individual mechanistic steps, we made use of a reconstituted system based on two individual constructs bearing either the N−terminal (NBD1) or the C−terminal AAA+ domain (NBD2). In contrast to the C−terminal construct, the N−terminal construct does not bind the fluorescent nucleotide MANT−dADP in isolation. However, sequential mixing experiments suggest that NBD1 obtains nucleotide binding competence when incorporated into an oligomeric complex. These findings support a model in which nucleotide binding to NBD1 is dependent on and regulated by trans−acting elements from neighboring subunits, either by direct interaction with the nucleotide or by stabilization of a nucleotide binding−competent state. In this way, they provide a basis for intersubunit communication within the functional ClpB complex

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Sprache(n): eng - English
 Datum: 2010-12-222010-11-152010-12-232011-02-08
 Publikationsstatus: Erschienen
 Seiten: 11
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 Art der Begutachtung: Expertenbegutachtung
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Titel: Biochemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Columbus, Ohio : American Chemical Society
Seiten: - Band / Heft: 50 (5) Artikelnummer: - Start- / Endseite: 899 - 909 Identifikator: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103