Signal recognition particle (SRP)- mediated targeting and Sec-dependent translocation of an extracellular E. coli protein.

R. Sijbrandi, M.L. Urbanus, C.M. ten Hagen-Jongman ten, H.D. Bernstein, B. Oudega, B.R. Otto, S. Luirink

Research output: Contribution to JournalArticleAcademic

Abstract

Hemoglobin protease (Hbp) is a hemoglobin-degrading protein that is secreted by a human pathogenic Escherichia coli strain via the autotransporter mechanism. Little is known about the earliest steps in autotransporter secretion, i.e. the targeting to and translocation across the inner membrane. Here, we present evidence that Hbp interacts with the signal recognition particle (SRP) and the Sec-translocon early during biogenesis. Furthermore, Hbp requires a functional SRP targeting pathway and Sec-translocon for optimal translocation across the inner membrane. SecB is not required for targeting of Hbp but can compensate to some extent for the lack of SRP. Hbp is synthesized with an unusually long signal peptide that is remarkably conserved among a subset of autotransporters. We propose that these autotransporters preferentially use the cotranslational SRP/Sec route to avoid adverse effects of the exposure of their mature domains in the cytoplasm.
Original languageEnglish
Pages (from-to)4654-4659
Number of pages6
JournalJournal of Biological Chemistry
Volume278
DOIs
Publication statusPublished - 2003

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Signal Recognition Particle
Escherichia coli Proteins
Hemoglobins
Peptide Hydrolases
Membranes
Protein Sorting Signals
Escherichia coli
Cytoplasm
Type V Secretion Systems

Cite this

@article{fd0e2de76c6b4d6999e4455bfa623027,
title = "Signal recognition particle (SRP)- mediated targeting and Sec-dependent translocation of an extracellular E. coli protein.",
abstract = "Hemoglobin protease (Hbp) is a hemoglobin-degrading protein that is secreted by a human pathogenic Escherichia coli strain via the autotransporter mechanism. Little is known about the earliest steps in autotransporter secretion, i.e. the targeting to and translocation across the inner membrane. Here, we present evidence that Hbp interacts with the signal recognition particle (SRP) and the Sec-translocon early during biogenesis. Furthermore, Hbp requires a functional SRP targeting pathway and Sec-translocon for optimal translocation across the inner membrane. SecB is not required for targeting of Hbp but can compensate to some extent for the lack of SRP. Hbp is synthesized with an unusually long signal peptide that is remarkably conserved among a subset of autotransporters. We propose that these autotransporters preferentially use the cotranslational SRP/Sec route to avoid adverse effects of the exposure of their mature domains in the cytoplasm.",
author = "R. Sijbrandi and M.L. Urbanus and {ten Hagen-Jongman ten}, C.M. and H.D. Bernstein and B. Oudega and B.R. Otto and S. Luirink",
year = "2003",
doi = "10.1074/jbc.M211630200",
language = "English",
volume = "278",
pages = "4654--4659",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

Signal recognition particle (SRP)- mediated targeting and Sec-dependent translocation of an extracellular E. coli protein. / Sijbrandi, R.; Urbanus, M.L.; ten Hagen-Jongman ten, C.M.; Bernstein, H.D.; Oudega, B.; Otto, B.R.; Luirink, S.

In: Journal of Biological Chemistry, Vol. 278, 2003, p. 4654-4659.

Research output: Contribution to JournalArticleAcademic

TY - JOUR

T1 - Signal recognition particle (SRP)- mediated targeting and Sec-dependent translocation of an extracellular E. coli protein.

AU - Sijbrandi, R.

AU - Urbanus, M.L.

AU - ten Hagen-Jongman ten, C.M.

AU - Bernstein, H.D.

AU - Oudega, B.

AU - Otto, B.R.

AU - Luirink, S.

PY - 2003

Y1 - 2003

N2 - Hemoglobin protease (Hbp) is a hemoglobin-degrading protein that is secreted by a human pathogenic Escherichia coli strain via the autotransporter mechanism. Little is known about the earliest steps in autotransporter secretion, i.e. the targeting to and translocation across the inner membrane. Here, we present evidence that Hbp interacts with the signal recognition particle (SRP) and the Sec-translocon early during biogenesis. Furthermore, Hbp requires a functional SRP targeting pathway and Sec-translocon for optimal translocation across the inner membrane. SecB is not required for targeting of Hbp but can compensate to some extent for the lack of SRP. Hbp is synthesized with an unusually long signal peptide that is remarkably conserved among a subset of autotransporters. We propose that these autotransporters preferentially use the cotranslational SRP/Sec route to avoid adverse effects of the exposure of their mature domains in the cytoplasm.

AB - Hemoglobin protease (Hbp) is a hemoglobin-degrading protein that is secreted by a human pathogenic Escherichia coli strain via the autotransporter mechanism. Little is known about the earliest steps in autotransporter secretion, i.e. the targeting to and translocation across the inner membrane. Here, we present evidence that Hbp interacts with the signal recognition particle (SRP) and the Sec-translocon early during biogenesis. Furthermore, Hbp requires a functional SRP targeting pathway and Sec-translocon for optimal translocation across the inner membrane. SecB is not required for targeting of Hbp but can compensate to some extent for the lack of SRP. Hbp is synthesized with an unusually long signal peptide that is remarkably conserved among a subset of autotransporters. We propose that these autotransporters preferentially use the cotranslational SRP/Sec route to avoid adverse effects of the exposure of their mature domains in the cytoplasm.

U2 - 10.1074/jbc.M211630200

DO - 10.1074/jbc.M211630200

M3 - Article

VL - 278

SP - 4654

EP - 4659

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -