Flexibility in targeting and insertion during bacterial membrane protein biogenesis.

D.W. van Bloois, C.M. ten Hagen-Jongman, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The biogenesis of Escherichia coli inner membrane proteins (IMPs) is assisted by targeting and insertion factors such as the signal recognition particle (SRP), the Sec-translocon and YidC with translocation of (large) periplasmic domains energized by SecA and the proton motive force (pmf). The use of these factors and forces is probably primarily determined by specific structural features of an IMP. To analyze these features we have engineered a set of model IMPs based on endogenous E. coli IMPs known to follow distinct targeting and insertion pathways. The modified model IMPs were analyzed for altered routing using an in vivo protease mapping approach. The data suggest a facultative use of different combinations of factors. © 2007 Elsevier Inc. All rights reserved.
LanguageEnglish
Pages727-733
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume362
DOIs
Publication statusPublished - 2009

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Bacterial Proteins
Membrane Proteins
Signal Recognition Particle
Proton-Motive Force
Escherichia coli
Protons
Peptide Hydrolases

Cite this

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title = "Flexibility in targeting and insertion during bacterial membrane protein biogenesis.",
abstract = "The biogenesis of Escherichia coli inner membrane proteins (IMPs) is assisted by targeting and insertion factors such as the signal recognition particle (SRP), the Sec-translocon and YidC with translocation of (large) periplasmic domains energized by SecA and the proton motive force (pmf). The use of these factors and forces is probably primarily determined by specific structural features of an IMP. To analyze these features we have engineered a set of model IMPs based on endogenous E. coli IMPs known to follow distinct targeting and insertion pathways. The modified model IMPs were analyzed for altered routing using an in vivo protease mapping approach. The data suggest a facultative use of different combinations of factors. {\circledC} 2007 Elsevier Inc. All rights reserved.",
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Flexibility in targeting and insertion during bacterial membrane protein biogenesis. / van Bloois, D.W.; ten Hagen-Jongman, C.M.; Luirink, S.

In: Biochemical and Biophysical Research Communications, Vol. 362, 2009, p. 727-733.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Flexibility in targeting and insertion during bacterial membrane protein biogenesis.

AU - van Bloois, D.W.

AU - ten Hagen-Jongman, C.M.

AU - Luirink, S.

PY - 2009

Y1 - 2009

N2 - The biogenesis of Escherichia coli inner membrane proteins (IMPs) is assisted by targeting and insertion factors such as the signal recognition particle (SRP), the Sec-translocon and YidC with translocation of (large) periplasmic domains energized by SecA and the proton motive force (pmf). The use of these factors and forces is probably primarily determined by specific structural features of an IMP. To analyze these features we have engineered a set of model IMPs based on endogenous E. coli IMPs known to follow distinct targeting and insertion pathways. The modified model IMPs were analyzed for altered routing using an in vivo protease mapping approach. The data suggest a facultative use of different combinations of factors. © 2007 Elsevier Inc. All rights reserved.

AB - The biogenesis of Escherichia coli inner membrane proteins (IMPs) is assisted by targeting and insertion factors such as the signal recognition particle (SRP), the Sec-translocon and YidC with translocation of (large) periplasmic domains energized by SecA and the proton motive force (pmf). The use of these factors and forces is probably primarily determined by specific structural features of an IMP. To analyze these features we have engineered a set of model IMPs based on endogenous E. coli IMPs known to follow distinct targeting and insertion pathways. The modified model IMPs were analyzed for altered routing using an in vivo protease mapping approach. The data suggest a facultative use of different combinations of factors. © 2007 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.bbrc.2007.08.053

DO - 10.1016/j.bbrc.2007.08.053

M3 - Article

VL - 362

SP - 727

EP - 733

JO - Biochemical and Biophysical Research Communications

T2 - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

ER -