The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions

Molecular Microbiology
K R HardieA P Pugsley

Abstract

The chaperone-like protein of the main terminal branch of the general secretory pathway from Klebsiella oxytoca, the outer membrane lipoprotein PulS, protects the multimeric secretin PulD from degradation and promotes its correct localization to the outer membrane. To determine whether these are separable functions, or whether resistance to proteolysis results simply from correct localization of PulD, we replaced the lipoprotein-type signal peptide of PulS by the signal peptide of periplasmic maltose-binding protein. The resulting periplasmic PulS retained its ability to protect PulD, but not its ability to localize PulD to the outer membrane and to function in pullulanase secretion. Periplasmic PulS competed with wild-type PulS to prevent pullulanase secretion, presumably again by causing mislocalization of PulD. A hybrid protein comprising the mature part of PulS fused to the C-terminus of full-length maltose-binding protein (MalE-PulS) had similar properties to the periplasmic PulS protein. Moreover, MalE-PulS was shown to associate with PulD by amylose-affinity chromatography. The MalE-PulS hybrid was rendered completely functional (i.e. it restored pullulanase secretion in a pulS mutant) by replacing its signal peptide wit...Continue Reading

Citations

Apr 2, 2013·Research in Microbiology·S Peter Howard
Apr 10, 2013·Research in Microbiology·Séverine CollinAnthony P Pugsley
Feb 5, 2002·Microbes and Infection·Tyler G Kimbrough, Samuel I Miller
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Sep 23, 2008·Journal of Bacteriology·Marie-Stéphanie AschtgenEric Cascales
Nov 4, 2008·Journal of Bacteriology·Nienke BuddelmeijerAnthony P Pugsley
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Dec 14, 2004·Microbiology and Molecular Biology Reviews : MMBR·Ian R HendersonDlawer Ala'Aldeen
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Mar 25, 2006·Molecular Microbiology·Nicolas BayanAnthony P Pugsley

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