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Type III protein translocase : HrcN is a peripheral ATPase that is activated by oligomerization

Pozidis, Charalambos and Chalkiadaki, Aggeliki and Gomez-Serrano, Amalia and Stahlberg, Henning and Brown, Ian and Tampakaki, Anastasia P. and Lustig, Ariel and Sianidis, Giorgos and Politou, Anastasia S. and Engel, Andreas and Panopoulos, Nickolas J. and Mansfield, John and Pugsley, Anthony P. and Karamanou, Spyridoula and Economou, Anastassios. (2003) Type III protein translocase : HrcN is a peripheral ATPase that is activated by oligomerization. Journal of biological chemistry, Vol. 278, H. 28. pp. 25816-25824.

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Official URL: http://edoc.unibas.ch/dok/A5262399

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Abstract

Type III protein secretion (TTS) is catalyzed by translocases that span both membranes of Gram-negative bacteria. A hydrophilic TTS component homologous to F1/V1-ATPases is ubiquitous and essential for secretion. We show that hrcN encodes the putative TTS ATPase of Pseudomonas syringae pathovar phaseolicola and that HrcN is a peripheral protein that assembles in clusters at the membrane. A decahistidinyl HrcN derivative was overexpressed in Escherichia coli and purified to homogeneity in a folded state. Hydrodynamic analysis, cross-linking, and electron microscopy revealed four distinct HrcN forms: I, 48 kDa (monomer); II, approximately 300 kDa (putative hexamer); III, 575 kDa (dodecamer); and IV, approximately 3.5 MDa. Form III is the predominant form of HrcN at the membrane, and its ATPase activity is dramatically stimulated (<700-fold) over the basal activity of Form I. We propose that TTS ATPases catalyze protein translocation as activated homo-oligomers at the plasma membrane.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Society of Biological Chemists
ISSN:0021-9258
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:55
Deposited On:08 Jun 2012 06:45

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