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Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.
J Biochem 1998; 124(1):122-9JB

Abstract

Protein translocation across the cytoplasmic membrane of Escherichia coli is accomplished by concerted actions of the translocation ATPase SecA and the membrane-embedded SecE/Y/G complex. SecA interacts with preproteins and undergoes ATP-driven cycles of membrane insertion-deinsertion. To address how SecA interacts functionally with other components in the translocation machinery, we characterized a SecA mutant lacking amino-terminal 8 amino acid residues (SecA N-8). Although the absence of the 8 residues did not grossly affect the interaction of SecA with a preprotein, ATP, or phospholipids, nor did it affect the intrinsic ATPase activity, it gave differential effects on the translocation of different preproteins. It also affected the translocation ATPase activity, the ability of membrane insertion, and the topology inversion of SecG coupled with the membrane insertion-deinsertion of SecA. Most noteworthy, SecA N-8 was pronouncedly defective in the translocation of proton motive force-dependent preproteins, in which SecG might have a role. We propose that the amino-terminal region of SecA is important for the functional interaction with SecG.

Authors+Show Affiliations

School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, 192-0392, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9644254

Citation

Mori, H, et al. "Amino-terminal Region of SecA Is Involved in the Function of SecG for Protein Translocation Into Escherichia Coli Membrane Vesicles." Journal of Biochemistry, vol. 124, no. 1, 1998, pp. 122-9.
Mori H, Sugiyama H, Yamanaka M, et al. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. J Biochem. 1998;124(1):122-9.
Mori, H., Sugiyama, H., Yamanaka, M., Sato, K., Tagaya, M., & Mizushima, S. (1998). Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Journal of Biochemistry, 124(1), pp. 122-9.
Mori H, et al. Amino-terminal Region of SecA Is Involved in the Function of SecG for Protein Translocation Into Escherichia Coli Membrane Vesicles. J Biochem. 1998;124(1):122-9. PubMed PMID: 9644254.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. AU - Mori,H, AU - Sugiyama,H, AU - Yamanaka,M, AU - Sato,K, AU - Tagaya,M, AU - Mizushima,S, PY - 1998/6/30/pubmed PY - 1998/6/30/medline PY - 1998/6/30/entrez SP - 122 EP - 9 JF - Journal of biochemistry JO - J. Biochem. VL - 124 IS - 1 N2 - Protein translocation across the cytoplasmic membrane of Escherichia coli is accomplished by concerted actions of the translocation ATPase SecA and the membrane-embedded SecE/Y/G complex. SecA interacts with preproteins and undergoes ATP-driven cycles of membrane insertion-deinsertion. To address how SecA interacts functionally with other components in the translocation machinery, we characterized a SecA mutant lacking amino-terminal 8 amino acid residues (SecA N-8). Although the absence of the 8 residues did not grossly affect the interaction of SecA with a preprotein, ATP, or phospholipids, nor did it affect the intrinsic ATPase activity, it gave differential effects on the translocation of different preproteins. It also affected the translocation ATPase activity, the ability of membrane insertion, and the topology inversion of SecG coupled with the membrane insertion-deinsertion of SecA. Most noteworthy, SecA N-8 was pronouncedly defective in the translocation of proton motive force-dependent preproteins, in which SecG might have a role. We propose that the amino-terminal region of SecA is important for the functional interaction with SecG. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/9644254/Amino_terminal_region_of_SecA_is_involved_in_the_function_of_SecG_for_protein_translocation_into_Escherichia_coli_membrane_vesicles_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/124.122?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -