The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.

W.S.P. Jong; S. Luirink

doi:10.1016/j.bbrc.2008.01.122

The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Autotransporters (ATs) of Gram-negative bacteria are often produced with an unusual signal peptide that carries a conserved N-terminal extension. Using combined in vitro and in vivo approaches we show that the extension of the AT hemoglobin protease (Hbp) does not affect targeting of Hbp via the SRP-pathway, suggesting that the extension is not involved in targeting pathway selection. © 2008 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	522-527
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	368
DOIs	https://doi.org/10.1016/j.bbrc.2008.01.122
Publication status	Published - 2008

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title = "The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.",

abstract = "Autotransporters (ATs) of Gram-negative bacteria are often produced with an unusual signal peptide that carries a conserved N-terminal extension. Using combined in vitro and in vivo approaches we show that the extension of the AT hemoglobin protease (Hbp) does not affect targeting of Hbp via the SRP-pathway, suggesting that the extension is not involved in targeting pathway selection. {\textcopyright} 2008 Elsevier Inc. All rights reserved.",

author = "W.S.P. Jong and S. Luirink",

year = "2008",

doi = "10.1016/j.bbrc.2008.01.122",

language = "English",

volume = "368",

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journal = "Biochemical and Biophysical Research Communications",

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publisher = "Academic Press Inc.",

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T1 - The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.

AU - Jong, W.S.P.

AU - Luirink, S.

PY - 2008

Y1 - 2008

N2 - Autotransporters (ATs) of Gram-negative bacteria are often produced with an unusual signal peptide that carries a conserved N-terminal extension. Using combined in vitro and in vivo approaches we show that the extension of the AT hemoglobin protease (Hbp) does not affect targeting of Hbp via the SRP-pathway, suggesting that the extension is not involved in targeting pathway selection. © 2008 Elsevier Inc. All rights reserved.

AB - Autotransporters (ATs) of Gram-negative bacteria are often produced with an unusual signal peptide that carries a conserved N-terminal extension. Using combined in vitro and in vivo approaches we show that the extension of the AT hemoglobin protease (Hbp) does not affect targeting of Hbp via the SRP-pathway, suggesting that the extension is not involved in targeting pathway selection. © 2008 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.bbrc.2008.01.122

DO - 10.1016/j.bbrc.2008.01.122

M3 - Article

SN - 0006-291X

VL - 368

SP - 522

EP - 527

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

ER -

The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.

Abstract

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