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  trans-acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication

Zeymer, C., Fischer, S., & Reinstein, J. (2014). trans-acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication. The Journal of Biological Chemistry, 289(47), 32965-32976. doi:10.1074/jbc.M114.608828.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-55A5-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-1F9D-D
Genre: Journal Article

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 Creators:
Zeymer, Cathleen1, Author              
Fischer, Sebastian1, Author              
Reinstein, Jochen1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: ATPase; ATPases Associated with Diverse Cellular Activities (AAA); Allosteric Regulation; Arginine Finger; ClpB; Hsp104; Molecular Chaperone; Nucleotide Binding; Oligomerization
 Abstract: The molecular chaperone ClpB/Hsp104, a member of the AAA+ superfamily (ATPases associated with various cellular activities), rescues proteins from the aggregated state in collaboration with the DnaK/Hsp70 chaperone system. ClpB/Hsp104 forms a hexameric, ring-shaped complex that functions as a tightly regulated, ATP-powered molecular disaggregation machine. Highly conserved and essential arginine residues, often called arginine fingers, are located at the subunit interfaces of the complex, which also harbor the catalytic sites. Several AAA+ proteins, including ClpB/Hsp104, possess a pair of such trans-acting arginines in the N-terminal nucleotide binding domain (NBD1), both of which were shown to be crucial for oligomerization and ATPase activity. Here, we present a mechanistic study elucidating the role of this conserved arginine pair. First, we found that the arginines couple nucleotide binding to oligomerization of NBD1, which is essential for the activity. Next, we designed a set of covalently linked, dimeric ClpB NBD1 variants, carrying single subunits deficient in either ATP binding or hydrolysis, to study allosteric regulation and intersubunit communication. Using this well defined environment of site-specifically modified, cross-linked AAA+ domains, we found that the conserved arginine pair mediates the cooperativity of ATP binding and hydrolysis in an allosteric fashion.

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Language(s): eng - English
 Dates: 2014-09-012014-09-212014-09-242014-09-21
 Publication Status: Published in print
 Pages: 12
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 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 289 (47) Sequence Number: - Start / End Page: 32965 - 32976 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1