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, L. Froderberg, E.N.G. Houben, M.L. Urbanus, C. G. de Koster, J.W. de Gier, J. Luirink

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. Structured summary: MINT-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). © 2008.
LanguageEnglish
Pages1419-1424
JournalFEBS Letters
Volume2008
Issue number582
DOIs
Publication statusPublished - 2008

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Quality Control
Quality control
Membrane Proteins
Membranes
Escherichia coli
Modulators
Proteins
Peptide Hydrolases
E coli inner membrane protein
In Vitro Techniques

Cite this

van Bloois, E. ; Dekker, H.L. ; Froderberg, L. ; Houben, E.N.G. ; Urbanus, M.L. ; de Koster, C. G. ; de Gier, J.W. ; Luirink, J. / 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. In: FEBS Letters. 2008 ; Vol. 2008, No. 582. pp. 1419-1424.
@article{fc5315185e35444bb74e1eda438b64c3,
title = "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",
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. Structured summary: MINT-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). {\circledC} 2008.",
author = "{van Bloois}, E. and H.L. Dekker and L. Froderberg and E.N.G. Houben and M.L. Urbanus and {de Koster}, {C. G.} and {de Gier}, J.W. and J. Luirink",
year = "2008",
doi = "10.1016/j.febslet.2008.02.082",
language = "English",
volume = "2008",
pages = "1419--1424",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "582",

}

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

In: FEBS Letters, Vol. 2008, No. 582, 2008, p. 1419-1424.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - 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

AU - van Bloois, E.

AU - Dekker, H.L.

AU - Froderberg, L.

AU - Houben, E.N.G.

AU - Urbanus, M.L.

AU - de Koster, C. G.

AU - de Gier, J.W.

AU - Luirink, J.

PY - 2008

Y1 - 2008

N2 - 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 summary: MINT-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). © 2008.

AB - 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 summary: MINT-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). © 2008.

U2 - 10.1016/j.febslet.2008.02.082

DO - 10.1016/j.febslet.2008.02.082

M3 - Article

VL - 2008

SP - 1419

EP - 1424

JO - FEBS Letters

T2 - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 582

ER -