Title: Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
Authors: Pozidis, Charalambos ×
Chalkiadaki, Aggeliki
Gomez-Serrano, Amalia
Stahlberg, Henning
Brown, Ian
Tampakaki, Anastasia P
Lustig, Ariel
Sianidis, Giorgos
Politou, Anastasia S
Engel, Andreas
Panopoulos, Nickolas J
Mansfield, John
Pugsley, Anthony P
Karamanou, Spyridoula
Economou, Anastassios #
Issue Date: Jul-2003
Publisher: American Society for Biochemistry and Molecular Biology
Series Title: Journal of Biological Chemistry vol:278 issue:28 pages:25816-24
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.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science