Specificity of Lipoprotein Chaperones for the Characteristic Lipidated Structural Motifs of their Cognate Lipoproteins |
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| Authors: | Dr Tom Mejuch Dr Hilde van Hattum Dr Gemma Triola Dr Mamta Jaiswal Prof Dr Herbert Waldmann |
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| Affiliation: | 1. Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany;2. Department of Structural Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany;3. Department of Chemistry and Chemical Biology, Technical University of Dortmund, Dortmund, Germany |
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| Abstract: | Lipoprotein‐binding chaperones mediate intracellular transport of lipidated proteins and determine their proper localisation and functioning. Understanding of the exact structural parameters that determine recognition and transport by different chaperones is of major interest. We have synthesised several lipid‐modified peptides, representative of different lipoprotein classes, and have investigated their binding to the relevant chaperones PDEδ, UNC119a, UNC119b, and galectins‐1 and ‐3. Our results demonstrate that PDEδ recognises S‐isoprenylated C‐terminal peptidic structures but not N‐myristoylated peptides. In contrast, UNC119 proteins bind only mono‐N‐myristoylated, but do not recognise doubly lipidated and S‐isoprenylated peptides at the C terminus. For galectins‐1 and ‐3, neither binding to N‐acylated, nor to C‐terminally prenylated peptides could be determined. These results shed light on the specificity of the chaperone‐mediated cellular lipoprotein transport systems. |
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| Keywords: | fluorescent probes peptides protein modifications protein– protein interactions |
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