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J Biol Chem, Vol. 274, Issue 48, 34219-34225, November 26, 1999

Substrate Specificity of the SecB Chaperone

Nicola T. M. KnoblauchDagger , Stefan RüdigerDagger , Hans-Joachim Schönfeld§, Arnold J. M. Driessen, Jens Schneider-Mergenerparallel , and Bernd BukauDagger

From the Dagger  Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Straße 7, D-79104 Freiburg, Germany, § F. Hoffmann-La Roche Ltd., Pharmaceutical Research-Infectious Diseases, CH-4070 Basel, Switzerland, the  Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, and the parallel  Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt Universität zu Berlin, Schumannstraße 20-21, D-10098 Berlin, Germany

The bacterial chaperone SecB assists translocation of proteins across the inner membrane. The mechanism by which it differentiates between secretory and cytosolic proteins is poorly understood. To identify its binding motif, we screened 2688 peptides covering sequences of 23 proteins for SecB binding. The motif is ~9 residues long and is enriched in aromatic and basic residues, whereas acidic residues are disfavored. Its identification allows the prediction of binding regions within protein sequences with up to 87% accuracy. SecB-binding regions occur statistically every 20-30 residues. The occurrence and affinity of binding regions are similar in SecB-dependent and -independent secretory proteins and in cytosolic proteins, and SecB lacks specificity toward signal sequences. SecB cannot thus differentiate between secretory and non-secretory proteins via its binding specificity. This conclusion is supported by the finding that SecB binds denatured luciferase, thereby allowing subsequent refolding by the DnaK system. SecB may rather be a general chaperone whose involvement in translocation is mediated by interactions of SecB and signal sequences of SecB-bound preproteins with the translocation apparatus.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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