Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins

E. van Bloois, H.L. Dekker, E.N.G. Houben, M.L. Urbanus, C.G. de Koster, J.W. de Gier, J. Luirink, L. Froderberg, Linda Fröderberg

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Little is known about the quality control of proteins upon integration in the inner membrane of Escherichia coli. Here, we demonstrate that YidC and FtsH are adjacent to a nascent, truncated membrane protein using in vitro photo cross-linking. YidC plays a critical but poorly understood role in the biogenesis of E. coli inner membrane proteins (IMPs). FtsH functions as a membrane chaperone and protease. Furthermore, we show that FtsH and its modulator proteins HflK and HflC copurify with tagged YidC and, vice versa, that YidC copurifies with tagged FtsH. These results suggest that FtsH and YidC have a linked role in the quality control of IMPs.
Original languageUndefined/Unknown
Pages (from-to)1419-1424
JournalFEBS letters
Volume582
Issue number10
DOIs
Publication statusPublished - 2008

Cite this