Publication

Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation

Lycklama a Nijeholt, J. A., Bulacu, M., Marrink, S. J. & Driessen, A. J. M., 30-Jul-2010, In : The Journal of Biological Chemistry. 285, 31, p. 23747 - 23754 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to support the translocation of secretory proteins in their unfolded state. The SecY channel is closed at the periplasmic face of the membrane by a small re-entrance loop that connects transmembrane segment 1 with 2b. This helical domain 2a is termed the plug domain. By the introduction of pairs of cysteines and crosslinkers, the plug domain was immobilized inside the channel and connected to transmembrane segment 10. Translocation was inhibited to various degrees depending on the position and crosslinker spacer length. With one of the crosslinked mutants translocation occurred unrestricted. Biochemical characterization of this mutant as well as molecular dynamics simulations suggest that only a limited movement of the plug domain suffices for translocation.

Original languageEnglish
Pages (from-to)23747 - 23754
Number of pages8
JournalThe Journal of Biological Chemistry
Volume285
Issue number31
Publication statusPublished - 30-Jul-2010

    Keywords

  • ESCHERICHIA-COLI, CROSS-LINKING, CONDUCTING CHANNEL, PRECURSOR PROTEINS, FORCE-FIELD, MEMBRANE, PHENOTYPES, EFFICIENT, COMPLEX, PRLA

Download statistics

No data available

ID: 1933869