The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity.
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.
Jong
Wouter S P
WS
Department of Molecular Microbiology, Institute of Molecular Cell Biology, VU University Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands.
Luirink
Joen
J
D002462:Cell Membrane / Q000378:metabolism*; D017124:Conserved Sequence; D010450:Endopeptidases / Q000378:metabolism*; D048168:Escherichia coli K12 / Q000502:physiology*; D018390:Gene Targeting; D021382:Protein Sorting Signals / Q000502:physiology*; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D018271:Signal Recognition Particle / Q000378:metabolism*
D021382:Protein Sorting Signals; D018271:Signal Recognition Particle; D010450:Endopeptidases; C114676:hemoglobin protease Hbp