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Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation.
Cell 1996; 85(1):71-81Cell

Abstract

E. coli preprotein translocase comprises SecA and SecY/E/G complex. SecA delivers the preprotein to the putative protein-conducting channel formed by SecY/E by undergoing ATP-driven cycles of membrane insertion and deinsertion. SecG renders the translocase highly efficient. An antibody raised against the C-terminal region of SecG inhibits preprotein translocation into everted membrane vesicles despite the exposure of this region to the inside of membrane vesicles in the absence of preprotein translocation. When preprotein translocation was started with ATP and then blocked by the inhibition of ATP hydrolysis, the C-terminal region was exposed to the outside of membrane vesicles. Another region of SecG showed a change in membrane sidedness upon preprotein translocation, indicating that SecG undergoes topology inversion. This topology inversion was tightly coupled to the SecG function and linked with the insertion-deinsertion cycle of SecA.

Authors+Show Affiliations

Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8620539

Citation

Nishiyama, K, et al. "Inversion of the Membrane Topology of SecG Coupled With SecA-dependent Preprotein Translocation." Cell, vol. 85, no. 1, 1996, pp. 71-81.
Nishiyama K, Suzuki T, Tokuda H. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell. 1996;85(1):71-81.
Nishiyama, K., Suzuki, T., & Tokuda, H. (1996). Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell, 85(1), pp. 71-81.
Nishiyama K, Suzuki T, Tokuda H. Inversion of the Membrane Topology of SecG Coupled With SecA-dependent Preprotein Translocation. Cell. 1996 Apr 5;85(1):71-81. PubMed PMID: 8620539.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. AU - Nishiyama,K, AU - Suzuki,T, AU - Tokuda,H, PY - 1996/4/5/pubmed PY - 1996/4/5/medline PY - 1996/4/5/entrez SP - 71 EP - 81 JF - Cell JO - Cell VL - 85 IS - 1 N2 - E. coli preprotein translocase comprises SecA and SecY/E/G complex. SecA delivers the preprotein to the putative protein-conducting channel formed by SecY/E by undergoing ATP-driven cycles of membrane insertion and deinsertion. SecG renders the translocase highly efficient. An antibody raised against the C-terminal region of SecG inhibits preprotein translocation into everted membrane vesicles despite the exposure of this region to the inside of membrane vesicles in the absence of preprotein translocation. When preprotein translocation was started with ATP and then blocked by the inhibition of ATP hydrolysis, the C-terminal region was exposed to the outside of membrane vesicles. Another region of SecG showed a change in membrane sidedness upon preprotein translocation, indicating that SecG undergoes topology inversion. This topology inversion was tightly coupled to the SecG function and linked with the insertion-deinsertion cycle of SecA. SN - 0092-8674 UR - https://www.unboundmedicine.com/medline/citation/8620539/Inversion_of_the_membrane_topology_of_SecG_coupled_with_SecA_dependent_preprotein_translocation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0092-8674(00)81083-1 DB - PRIME DP - Unbound Medicine ER -