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Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.
EMBO J 1997; 16(10):2756-68EJ

Abstract

Escherichia coli preprotein translocase contains a membrane-embedded trimeric complex of SecY, SecE and SecG (SecYEG) and the peripheral SecA protein. SecYE is the conserved functional 'core' of the SecYEG complex. Although sufficient to provide sites for high-affinity binding and membrane insertion of SecA, and for its activation as a preprotein-dependent ATPase, SecYE has only very low capacity to support translocation. The proteins encoded by the secD operon--SecD, SecF and YajC--also form an integral membrane heterotrimeric complex (SecDFyajC). Physical and functional studies show that these two trimeric complexes are associated to form SecYEGDFyajC, the hexameric integral membrane domain of the preprotein translocase 'holoenzyme'. Either SecG or SecDFyajC can support the translocation activity of SecYE by facilitating the ATP-driven cycle of SecA membrane insertion and de-insertion at different stages of the translocation reaction. Our findings show that each of the prokaryote-specific subunits (SecA, SecG and SecDFyajC) function together to promote preprotein movement at the SecYE core of the translocase.

Authors+Show Affiliations

Dartmouth Medical School, Department of Biochemistry, Hanover, NH 03755, USA.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9184221

Citation

Duong, F, and W Wickner. "Distinct Catalytic Roles of the SecYE, SecG and SecDFyajC Subunits of Preprotein Translocase Holoenzyme." The EMBO Journal, vol. 16, no. 10, 1997, pp. 2756-68.
Duong F, Wickner W. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J. 1997;16(10):2756-68.
Duong, F., & Wickner, W. (1997). Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. The EMBO Journal, 16(10), pp. 2756-68.
Duong F, Wickner W. Distinct Catalytic Roles of the SecYE, SecG and SecDFyajC Subunits of Preprotein Translocase Holoenzyme. EMBO J. 1997 May 15;16(10):2756-68. PubMed PMID: 9184221.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. AU - Duong,F, AU - Wickner,W, PY - 1997/5/15/pubmed PY - 1997/5/15/medline PY - 1997/5/15/entrez SP - 2756 EP - 68 JF - The EMBO journal JO - EMBO J. VL - 16 IS - 10 N2 - Escherichia coli preprotein translocase contains a membrane-embedded trimeric complex of SecY, SecE and SecG (SecYEG) and the peripheral SecA protein. SecYE is the conserved functional 'core' of the SecYEG complex. Although sufficient to provide sites for high-affinity binding and membrane insertion of SecA, and for its activation as a preprotein-dependent ATPase, SecYE has only very low capacity to support translocation. The proteins encoded by the secD operon--SecD, SecF and YajC--also form an integral membrane heterotrimeric complex (SecDFyajC). Physical and functional studies show that these two trimeric complexes are associated to form SecYEGDFyajC, the hexameric integral membrane domain of the preprotein translocase 'holoenzyme'. Either SecG or SecDFyajC can support the translocation activity of SecYE by facilitating the ATP-driven cycle of SecA membrane insertion and de-insertion at different stages of the translocation reaction. Our findings show that each of the prokaryote-specific subunits (SecA, SecG and SecDFyajC) function together to promote preprotein movement at the SecYE core of the translocase. SN - 0261-4189 UR - https://www.unboundmedicine.com/medline/citation/9184221/Distinct_catalytic_roles_of_the_SecYE_SecG_and_SecDFyajC_subunits_of_preprotein_translocase_holoenzyme_ L2 - http://emboj.embopress.org/cgi/pmidlookup?view=long&pmid=9184221 DB - PRIME DP - Unbound Medicine ER -