SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.

Rasha Younis; Lewis Bingle; S Rollauer; D Munera; Stephen Busby; S Johnson; JE Deane; SM Lea; G Frankel; Mark Pallen

doi:10.1128/JB.00760-10

SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.

Rasha Younis
, Lewis Bingle
, S Rollauer
, D Munera
, Stephen Busby
, S Johnson
, JE Deane
, SM Lea
, G Frankel
, Mark Pallen

Research output: Contribution to journal › Article

22 Citations (Scopus)

Abstract

Here we show that the type-III secretion gatekeeper protein SepL resembles an aberrant effector protein, in binding to a class 1 type-III secretion chaperone (ORF12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.

Original language	English
Journal	Journal of Bacteriology
DOIs	https://doi.org/10.1128/JB.00760-10
Publication status	Published - 10 Sept 2010

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10.1128/JB.00760-10

Ler, a versatile global regulator from E.coli O157 and related strains
Pallen, M. (Principal Investigator), Busby, S. (Co-Investigator) & Futterer, K. (Co-Investigator)
Biotechnology & Biological Sciences Research Council
1/07/07 → 30/06/10
Project: Research Councils
The Scatterlings of Virulence: Towards a Complete Type-III Secretion Effector Repertoire in Escherichia Coli
Pallen, M. (Principal Investigator) & Machesky, L. (Co-Investigator)
Biotechnology & Biological Sciences Research Council
1/02/06 → 31/01/09
Project: Research Councils

Cite this

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title = "SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.",

abstract = "Here we show that the type-III secretion gatekeeper protein SepL resembles an aberrant effector protein, in binding to a class 1 type-III secretion chaperone (ORF12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.",

author = "Rasha Younis and Lewis Bingle and S Rollauer and D Munera and Stephen Busby and S Johnson and JE Deane and SM Lea and G Frankel and Mark Pallen",

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doi = "10.1128/JB.00760-10",

language = "English",

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publisher = "American Society for Microbiology",

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T1 - SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.

AU - Younis, Rasha

AU - Bingle, Lewis

AU - Rollauer, S

AU - Munera, D

AU - Busby, Stephen

AU - Johnson, S

AU - Deane, JE

AU - Lea, SM

AU - Frankel, G

AU - Pallen, Mark

PY - 2010/9/10

Y1 - 2010/9/10

N2 - Here we show that the type-III secretion gatekeeper protein SepL resembles an aberrant effector protein, in binding to a class 1 type-III secretion chaperone (ORF12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.

AB - Here we show that the type-III secretion gatekeeper protein SepL resembles an aberrant effector protein, in binding to a class 1 type-III secretion chaperone (ORF12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.

U2 - 10.1128/JB.00760-10

DO - 10.1128/JB.00760-10

M3 - Article

C2 - 20833800

JO - Journal of Bacteriology

JF - Journal of Bacteriology

ER -

SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.

Abstract

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Ler, a versatile global regulator from E.coli O157 and related strains

The Scatterlings of Virulence: Towards a Complete Type-III Secretion Effector Repertoire in Escherichia Coli

Cite this