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

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.Structured summaryMINT-6478034:hflB (uniprotkb:P0AAI3) physically interacts (MI:0218) with yidC (uniprotkb:P25714), hflK (uniprotkb:P0ABC7), hflC (uniprotkb:P0ABC3) by cross-linking studies (MI:0030)MINT-6478363:yidC (uniprotkb:P25714) physically interacts (MI:0218) with lldD (uniprotkb:P33232), rplD (uniprotkb:P60723), yrbD (uniprotkb:P64604), rpsA (uniprotkb:P0AG67), aphA1 (uniprotkb:P00551), dacC (uniprotkb:P08506), rpsC (uniprotkb:P0A7V3), rpsD (uniprotkb:P0A7V8), rpsE (uniprotkb:P0A7W1), rpoA (uniprotkb:P0A7Z4), ompC (uniprotkb:P06996), ompA (uniprotkb:P0A910), atpA (uniprotkb:P0ABB0), atpD (uniprotkb:P0ABB4), adhE (uniprotkb:P0A9Q7),hflB (uniprotkb:P0AAI3), hflC (uniprotkb:P0ABC3), hflK (uniprotkb:P0ABC7), lacI (uniprotkb:P03023), gapA (uniprotkb:P0A9B2), rbsB (uniprotkb:P02925), sdhA (uniprotkb:P0AC41), rho (uniprotkb:P0AG30), udp (uniprotkb:P12758), nuoC (uniprotkb:P33599), treB (uniprotkb:P36672) and manX (uniprotkb:P69797) by cross-linking studies (MI:0030)MINT-6477988:yidC (uniprotkb:P25714) physically interacts (MI:0218) with hflB (uniprotkb:P0AAI3), hflK (uniprotkb:P0ABC7), hflC (uniprotkb:P0ABC3), secD (uniprotkb:P0AG90) and secG (uniprotkb:P0AG99) by cross-linking studies (MI:0030)MINT-6478012:yidC (uniprotkb:P25714) physically interacts (MI:0218) with hflC(uniprotkb:P0ABC3) and hflK (uniprotkb:P0ABC7) by cross-linking studies (MI:0030)