NDLI: Functional and structural characterization of the minimal Sec translocase of the hyperthermophile Thermotoga maritima

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Functional and structural characterization of the minimal Sec translocase of the hyperthermophile Thermotoga maritima

Content Provider	Springer Nature Link
Author	Pretz, Monika G. Remigy, Hervé Swaving, Jelto Albers, Sonja V. Garrido, Victoria G. Chami, Mohamed Engel, Andreas Driessen, Arld J. M.
Copyright Year	2005
Abstract	The genome of the hyperthermophilic bacterium Thermotoga maritima contains the genes that encode core subunits of the protein translocase, a complex consisting of the molecular motor SecA and the protein conducting pore SecYE. In addition, we identified an erroneous sequence in the genome encoding for a putative secG gene. The genes of the T. maritima translocase subunits were overexpressed in Escherichia coli and purified to homogeneity. T. maritima SecA showed a basal thermostable ATPase activity that was stimulated up to 4-fold by phospholipids with an optimum at 74°C. Membrane vesicles and proteoliposomes containing SecYE or SecYEG supported 2- to 4-fold stimulation of the precursor dependent SecA ATPase activity. Imaging of small two-dimensional crystals of the SecYE complex using electron microscopy showed square-shaped particles with a side-length of about 6 nm. These results demonstrate that in T. maritima a highly thermostable translocase complex is operational.
Starting Page	307
Ending Page	316
Page Count	10
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	9
Issue Number	4
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-05-14
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Thermophiles Protein translocation SecYEG SecA ATPase 2D-crystallization Lipid layer Electron microscopy
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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