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 E H Bingle; Sarah E. Rollauer; Diana Munera; Stephen JW Busby; Steven Johnson; Janet E Deane; Susan M. Lea; Gad Frankel; Mark J 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 E H Bingle, Sarah E. Rollauer, Diana Munera, Stephen JW Busby, Steven Johnson, Janet E Deane, Susan M. Lea, Gad Frankel, Mark J Pallen

Research output: Contribution to journal › Article › Research › peer-review

23 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
Pages (from-to)	6093-6098
Number of pages	6
Journal	Journal of Bacteriology
Volume	192
Issue number	22
DOIs	https://doi.org/10.1128/JB.00760-10
Publication status	Published - Nov 2010
Externally published	Yes

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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 Bingle, \{Lewis E H\} and Rollauer, \{Sarah E.\} and Diana Munera and Busby, \{Stephen JW\} and Steven Johnson and Deane, \{Janet E\} and Lea, \{Susan M.\} and Gad Frankel and Pallen, \{Mark J\}",

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

language = "English",

volume = "192",

pages = "6093--6098",

journal = "Journal of Bacteriology",

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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 E H

AU - Rollauer, Sarah E.

AU - Munera, Diana

AU - Busby, Stephen JW

AU - Johnson, Steven

AU - Deane, Janet E

AU - Lea, Susan M.

AU - Frankel, Gad

AU - Pallen, Mark J

PY - 2010/11

Y1 - 2010/11

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.

UR - https://www.scopus.com/pages/publications/78049445421

U2 - 10.1128/JB.00760-10

DO - 10.1128/JB.00760-10

M3 - Article

C2 - 20833800

AN - SCOPUS:78049445421

SN - 0021-9193

VL - 192

SP - 6093

EP - 6098

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 22

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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