| dc.creator |
Machón, Cristina |
|
| dc.creator |
Rivas, Susana |
|
| dc.creator |
Albert, Armando |
|
| dc.creator |
Goñi, Félix M. |
|
| dc.creator |
Cruz, Fernando de la |
|
| dc.date |
2008-04-14T09:35:28Z |
|
| dc.date |
2008-04-14T09:35:28Z |
|
| dc.date |
2002-03 |
|
| dc.date.accessioned |
2017-01-31T01:02:14Z |
|
| dc.date.available |
2017-01-31T01:02:14Z |
|
| dc.identifier |
Journal of Bacteriology 184(6): 1661–1668 (2002) |
|
| dc.identifier |
1098-5530 |
|
| dc.identifier |
http://hdl.handle.net/10261/3559 |
|
| dc.identifier |
10.1128/JB.184.6.1661-1668.2002 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3559 |
|
| dc.description |
TrwD, a hexameric ATP hydrolase encoded by plasmid R388, is a member of the PulE/VirB11 protein
superfamily of traffic ATPases. It is essential for plasmid conjugation, particularly for expression of the
conjugative W pilus. In the present study, we analyzed the effects that TrwD produced on unilamellar vesicles
consisting of cardiolipin and phosphatidylcholine in equimolar amounts. TrwD induced dose-dependent vesicle
aggregation and intervesicular mixing of the lipids located in the outer monolayers in the presence of calcium.
It also induced extensive leakage of the vesicular aqueous contents. A point mutant of TrwD with a mutation
in the P loop of the nucleotide-binding region (K203Q) that lacks both ATPase activity and the ability to
support conjugation showed the same behavior as native TrwD in all of these processes, which were independent
of the presence of ATP. Structure prediction methods revealed a close similarity to Helicobacter pylori
protein HP0525, another member of the PulE/VirB11 family, whose crystal structure is known. The interpretation
of our data in the light of this structure is that TrwD interacts with the lipid bilayer through hydrophobic
regions in its N-terminal domain, which leads to a certain degree of membrane destabilization. TrwD appears
to be a part of the conjugation machinery that interacts with the membranous systems in order to facilitate
DNA transfer in bacteria. |
|
| dc.description |
This work was supported with funds from DGICYT (grants PB98-
1106 to F.C. and PB96-0171 to F.M.G.), the Basque Government
(grants EX-98/28 and PI98/32 to F.M.G.), and the University of the
Basque Country (grant G03/98 to F.M.G.). C.M. and S.R. were predoctoral
students supported by the Basque Government. |
|
| dc.description |
Peer reviewed |
|
| dc.format |
208395 bytes |
|
| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
American Society for Microbiology |
|
| dc.relation |
http://dx.doi.org/10.1128/JB.184.6.1661-1668.2002 |
|
| dc.rights |
closedAccess |
|
| dc.title |
TrwD, the Hexameric Traffic ATPase Encoded by Plasmid R388, Induces Membrane Destabilization and Hemifusion of Lipid Vesicles |
|
| dc.type |
Artículo |
|