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Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner

Houben, E. N. G., Nouwen, N., Luirink, J., Driessen, A. J. M. & van der Laan, M., 2001, In : Embo Reports. 2, 6, p. 519-523 5 p.

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DOI

The inner membrane protein YidC is associated with the preprotein translocase of Escherichia coli and contacts transmembrane segments of nascent inner membrane proteins during membrane insertion. YidC was purified to homogeneity and co-reconstituted with the SecYEG complex. YidC had no effect on the SecA/SecYEG-mediated translocation of the secretory protein proOmpA; however, using a crosslinking approach, the transmembrane segment of nascent FtsQ was found to gain access to YidC via SecY. These data indicate the functional reconstitution of the initial stages of YidC-dependent membrane protein insertion via the SecYEG complex.
Original languageEnglish
Pages (from-to)519-523
Number of pages5
JournalEmbo Reports
Volume2
Issue number6
Publication statusPublished - 2001

    Keywords

  • SIGNAL RECOGNITION PARTICLE, ESCHERICHIA-COLI SRP, INNER MEMBRANE, TRIGGER FACTOR, TRANSLOCATION CHANNEL, ESSENTIAL COMPONENT, BACTERIAL PROTEIN, N-TERMINI, C-TERMINI, EXPORT

ID: 1217276