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.
authors.affiliation: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.
authors.forename: Rasha
authors.initials: R
authors.lastname: Younis
authors.forename: Lewis E H
authors.initials: LE
authors.lastname: Bingle
authors.forename: Sarah
authors.initials: S
authors.lastname: Rollauer
authors.forename: Diana
authors.initials: D
authors.lastname: Munera
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Busby
authors.forename: Steven
authors.initials: S
authors.lastname: Johnson
authors.forename: Janet E
authors.initials: JE
authors.lastname: Deane
authors.forename: Susan M
authors.initials: SM
authors.lastname: Lea
authors.forename: Gad
authors.initials: G
authors.lastname: Frankel
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Pallen
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D021382:Protein Sorting Signals; D021381:Protein Transport; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D021382:Protein Sorting Signals; C416081:SepL protein, E coli