AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ

AAA+ chaperone ClpX has been suggested to be a modulator of prokaryotic cytoskeletal protein FtsZ, but the details of recognition and remodeling of FtsZ by ClpX are largely unknown. In this study, we have extensively investigated the nature of FtsZ polymers and mechanisms of ClpX-regulated FtsZ poly...

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Bibliographic Details
Published in:The Journal of biological chemistry 2010-02, Vol.285 (9), p.6648-6657
Main Authors: Sugimoto, Shinya, Yamanaka, Kunitoshi, Nishikori, Shingo, Miyagi, Atsushi, Ando, Toshio, Ogura, Teru
Format: Article
Language:English
Subjects:
AAA+
Adenosine Triphosphatases - physiology
Adenosine Triphosphate
ATPases Associated with Diverse Cellular Activities
Bacterial Proteins - metabolism
Binding Sites
Cell/Division
Chaperones
Cytoskeletal Proteins - metabolism
Cytoskeleton
Endopeptidase Clp - physiology
Escherichia coli
Escherichia coli - cytology
Escherichia coli Proteins - physiology
High Speed AFM
Microscopy, Atomic Force
Molecular Chaperones - physiology
Polymerization
Protein Degradation
Protein Folding
Protein Multimerization
Protein Structure and Folding
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Summary:AAA+ chaperone ClpX has been suggested to be a modulator of prokaryotic cytoskeletal protein FtsZ, but the details of recognition and remodeling of FtsZ by ClpX are largely unknown. In this study, we have extensively investigated the nature of FtsZ polymers and mechanisms of ClpX-regulated FtsZ polymer dynamics. We found that FtsZ polymerization is inhibited by ClpX in an ATP-independent manner and that the N-terminal domain of ClpX plays a crucial role for the inhibition of FtsZ polymerization. Single molecule analysis with high speed atomic force microscopy directly revealed that FtsZ polymer is in a dynamic equilibrium between polymerization and depolymerization on a time scale of several seconds. ClpX disassembles FtsZ polymers presumably by blocking reassembly of FtsZ. Furthermore, Escherichia coli cells overproducing ClpX and N-terminal domain of ClpX show filamentous morphology with abnormal localization of FtsZ. These data together suggest that ClpX modulates FtsZ polymer dynamics in an ATP-independent fashion, which is achieved by interaction between the N-terminal domain of ClpX and FtsZ monomers or oligomers.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M109.080739