Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent mannerHouben, 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.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||5|
|Publication status||Published - 2001|
- SIGNAL RECOGNITION PARTICLE, ESCHERICHIA-COLI SRP, INNER MEMBRANE, TRIGGER FACTOR, TRANSLOCATION CHANNEL, ESSENTIAL COMPONENT, BACTERIAL PROTEIN, N-TERMINI, C-TERMINI, EXPORT