Work

SepL Resembles an Aberrant Effector in Binding to a Class 1 Type III Secretion Chaperone and Carrying an N-Terminal Secretion Signal

Year: 2010

Type: article

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.

Source: Journal of Bacteriology

DOI: 10.1128/jb.00760-10

Authors: Rasha Younis, Lewis E. H. Bingle, Sarah Rollauer, Diana Munera, Stephen J. Busby, Steven Johnson, Janet E. Deane, Susan M. Lea, Gad Frankel, Mark J. Pallen

Institutions: University of Birmingham, University of Oxford, Imperial College London

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: Biotechnology and Biological Sciences Research Council

Awards: G2612518263, G7172091275, The Scatterlings of Virulence: towards a complete type-III secretion effector repertoire in Escherichia coli, Ler a versatile global regulator from E. coli O157 and related strains

OpenAlex ID: W2084811980

FWCI: 1.851

Cites: 29

Cited by: 30

Related to: 10