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Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking.
J Biochem 2000; 128(1):129-37JB

Abstract

SecG, a membrane component of the protein translocation apparatus of Escherichia coli, undergoes membrane topology inversion, which is coupled to the membrane insertion and deinsertion cycle of SecA. Eighteen SecG derivatives possessing a single cysteine residue at various positions were constructed and expressed in a secG null mutant. All the SecG-Cys derivatives retained the SecG function, and stimulated protein translocation both in vivo and in vitro. Inverted membrane vesicles containing a SecG-Cys derivative were labeled with a membrane-permeable or -impermeable sulfhydryl reagent before or after solubilization with a detergent. The accessibility of these reagents to the cysteine residue of each derivative determined the topological arrangement of SecG in the membrane. Derivatives having the cysteine residue in the periplasmic region each existed as a homodimer crosslinked through disulfide bonds, indicating that two SecG molecules closely co-exist in a single translocation machinery. The crosslinking did not abolish the SecG function and the crosslinked SecG dimer underwent topology inversion upon protein translocation.

Authors+Show Affiliations

Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

10876167

Citation

Nagamori, S, et al. "Two SecG Molecules Present in a Single Protein Translocation Machinery Are Functional Even After Crosslinking." Journal of Biochemistry, vol. 128, no. 1, 2000, pp. 129-37.
Nagamori S, Nishiyama K, Tokuda H. Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking. J Biochem. 2000;128(1):129-37.
Nagamori, S., Nishiyama, K., & Tokuda, H. (2000). Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking. Journal of Biochemistry, 128(1), pp. 129-37.
Nagamori S, Nishiyama K, Tokuda H. Two SecG Molecules Present in a Single Protein Translocation Machinery Are Functional Even After Crosslinking. J Biochem. 2000;128(1):129-37. PubMed PMID: 10876167.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Two SecG molecules present in a single protein translocation machinery are functional even after crosslinking. AU - Nagamori,S, AU - Nishiyama,K, AU - Tokuda,H, PY - 2000/7/6/pubmed PY - 2000/10/21/medline PY - 2000/7/6/entrez SP - 129 EP - 37 JF - Journal of biochemistry JO - J. Biochem. VL - 128 IS - 1 N2 - SecG, a membrane component of the protein translocation apparatus of Escherichia coli, undergoes membrane topology inversion, which is coupled to the membrane insertion and deinsertion cycle of SecA. Eighteen SecG derivatives possessing a single cysteine residue at various positions were constructed and expressed in a secG null mutant. All the SecG-Cys derivatives retained the SecG function, and stimulated protein translocation both in vivo and in vitro. Inverted membrane vesicles containing a SecG-Cys derivative were labeled with a membrane-permeable or -impermeable sulfhydryl reagent before or after solubilization with a detergent. The accessibility of these reagents to the cysteine residue of each derivative determined the topological arrangement of SecG in the membrane. Derivatives having the cysteine residue in the periplasmic region each existed as a homodimer crosslinked through disulfide bonds, indicating that two SecG molecules closely co-exist in a single translocation machinery. The crosslinking did not abolish the SecG function and the crosslinked SecG dimer underwent topology inversion upon protein translocation. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/10876167/Two_SecG_molecules_present_in_a_single_protein_translocation_machinery_are_functional_even_after_crosslinking_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/128.129?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -