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Literature DB >> 19136590

ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.

Daniel P Haeusser¹, Amy H Lee, Richard B Weart, Petra Anne Levin.

Abstract

ClpX is a well-characterized bacterial chaperone that plays a role in many processes, including protein turnover and the remodeling of macromolecular complexes. All of these activities require ATP hydrolysis-dependent, ClpX-mediated protein unfolding. Here we used site-directed mutagenesis in combination with genetics and biochemistry to establish that ClpX inhibits assembly of the conserved division protein FtsZ through a noncanonical mechanism independent of its role as an ATP-dependent chaperone.

Entities: Chemical Gene

Mesh：

Substances：

Year: 2009 PMID： 19136590 PMCID： PMC2648377 DOI： 10.1128/JB.01606-07

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

33 in total

Review 1. Posttranslational quality control: folding, refolding, and degrading proteins.

Authors: S Wickner; M R Maurizi; S Gottesman
Journal: Science Date: 1999-12-03 Impact factor: 47.728

2. Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC.

Authors: A L Marston; J Errington
Journal: Mol Microbiol Date: 1999-07 Impact factor: 3.501

3. ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster.

Authors: Erin L Mettert; Patricia J Kiley
Journal: J Mol Biol Date: 2005-10-07 Impact factor: 5.469

Review 4. AAA+ proteins: have engine, will work.

Authors: Phyllis I Hanson; Sidney W Whiteheart
Journal: Nat Rev Mol Cell Biol Date: 2005-07 Impact factor: 94.444

5. The division inhibitor EzrA contains a seven-residue patch required for maintaining the dynamic nature of the medial FtsZ ring.

Authors: Daniel P Haeusser; Anna Cristina Garza; Amy Z Buscher; Petra Anne Levin
Journal: J Bacteriol Date: 2007-09-14 Impact factor: 3.490

ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.

Review 1. Posttranslational quality control: folding, refolding, and degrading proteins.

2. Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC.

3. ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster.

Review 4. AAA+ proteins: have engine, will work.

5. The division inhibitor EzrA contains a seven-residue patch required for maintaining the dynamic nature of the medial FtsZ ring.

6. A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator.

7. A metabolic sensor governing cell size in bacteria.

8. The RssB response regulator directly targets sigma(S) for degradation by ClpXP.

9. The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37 degrees C.

10. The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ.

1. ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics.

Review 2. Bacterial cell division: assembly, maintenance and disassembly of the Z ring.

3. AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ.

4. Proteomics analyses of Bacillus subtilis after treatment with plumbagin, a plant-derived naphthoquinone.

Review 5. Bacterial Cell Division: Nonmodels Poised to Take the Spotlight.

6. Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ.

7. The interplay of ClpXP with the cell division machinery in Escherichia coli.

8. FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis.

9. Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly.

10. ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.