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The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli.
J Biol Chem 1992; 267(10):7170-6JB

Abstract

Genes encoding the C- and N-terminal regions of SecE were constructed and placed under the control of the tac promoter on plasmids. The C-terminal region of SecE (SecE-C) was sufficient for suppression of the secEcs phenotype, confirming the results of Schatz et al. (Schatz, P. J., Bieker, K. L., Ottemann, K. M., Silhavy, T. J., and Beckwith, J. (1991) EMBO J. 10, 1749-1757). SecE-C allowed the overproduction of SecY, and its overproduction was achieved when the tac-secY gene, on a plasmid, was induced, indicating that the C-terminal region is the site of interaction of SecE with SecY and that the interaction makes the two Sec proteins stable. SecE-C was purified and used with SecY for the reconstitution of protein translocation activity. SecE-C was active in the functional reconstitution. The SecE-C/SecY-dependent protein translocation absolutely required SecA and ATP as the native translocation reaction did. Quantitative analysis revealed that SecE-C was 50% as active as intact SecE. The N-terminal region of SecE (SecE-N) also suppressed in vivo the defect caused by the secEcs mutation. SecE-N was, however, inactive in the overproduction of SecY. A possible oligomeric structure of SecE is discussed.

Authors+Show Affiliations

Institute of Applied Microbiology, 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

1551922

Citation

Nishiyama, K, et al. "The Carboxyl-terminal Region of SecE Interacts With SecY and Is Functional in the Reconstitution of Protein Translocation Activity in Escherichia Coli." The Journal of Biological Chemistry, vol. 267, no. 10, 1992, pp. 7170-6.
Nishiyama K, Mizushima S, Tokuda H. The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli. J Biol Chem. 1992;267(10):7170-6.
Nishiyama, K., Mizushima, S., & Tokuda, H. (1992). The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli. The Journal of Biological Chemistry, 267(10), pp. 7170-6.
Nishiyama K, Mizushima S, Tokuda H. The Carboxyl-terminal Region of SecE Interacts With SecY and Is Functional in the Reconstitution of Protein Translocation Activity in Escherichia Coli. J Biol Chem. 1992 Apr 5;267(10):7170-6. PubMed PMID: 1551922.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli. AU - Nishiyama,K, AU - Mizushima,S, AU - Tokuda,H, PY - 1992/4/5/pubmed PY - 1992/4/5/medline PY - 1992/4/5/entrez SP - 7170 EP - 6 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 267 IS - 10 N2 - Genes encoding the C- and N-terminal regions of SecE were constructed and placed under the control of the tac promoter on plasmids. The C-terminal region of SecE (SecE-C) was sufficient for suppression of the secEcs phenotype, confirming the results of Schatz et al. (Schatz, P. J., Bieker, K. L., Ottemann, K. M., Silhavy, T. J., and Beckwith, J. (1991) EMBO J. 10, 1749-1757). SecE-C allowed the overproduction of SecY, and its overproduction was achieved when the tac-secY gene, on a plasmid, was induced, indicating that the C-terminal region is the site of interaction of SecE with SecY and that the interaction makes the two Sec proteins stable. SecE-C was purified and used with SecY for the reconstitution of protein translocation activity. SecE-C was active in the functional reconstitution. The SecE-C/SecY-dependent protein translocation absolutely required SecA and ATP as the native translocation reaction did. Quantitative analysis revealed that SecE-C was 50% as active as intact SecE. The N-terminal region of SecE (SecE-N) also suppressed in vivo the defect caused by the secEcs mutation. SecE-N was, however, inactive in the overproduction of SecY. A possible oligomeric structure of SecE is discussed. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/1551922/The_carboxyl_terminal_region_of_SecE_interacts_with_SecY_and_is_functional_in_the_reconstitution_of_protein_translocation_activity_in_Escherichia_coli_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=1551922 DB - PRIME DP - Unbound Medicine ER -