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J. Biol. Chem., Vol. 278, Issue 29, 26639-26647, July 18, 2003

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Oligomerization, Membrane Anchoring, and Cellulose-binding Characteristics of AbpS, a Receptor-like Streptomyces Protein^*

Stefan Walter  and Hildgund Schrempf

From the Fachbereich B Biologie/Chemie, Universität Osnabrück, 49069 Osnabrück, Germany

Streptomyces reticuli produces a 34.6-kDa surface-anchored protein (AbpS) whose surface-exposed N terminus binds strongly to Avicel, a dominantly crystalline type of cellulose. The generation of a large set of mutated abpS-genes and the subsequent analysis of the corresponding proteins in vitro as well as in vivo in a Streptomyces host allow the assignment of the following characteristics for AbpS. (i) Amino acid residues participating directly in the cellulose-interaction are located at the N terminus. (ii) As ascertained by cross-linking experiments, AbpS forms homotetramers in its soluble as well as cellulose-bound form. (iii) The intermolecular assembly of four AbpS molecules is governed by two domains (including amino acids 60–110 and 161–212). Both domains possess large portions of -helical regions in which hydrophobic amino acids are located on one side as known from coiled-coil proteins. (iv) The C-terminal part of AbpS comprising 35 amino acids contains a transmembrane domain. Due to the surface-exposed N terminus of AbpS and the presence of transmembrane helix the C terminus has to be situated in the cytoplasm of the S. reticuli hyphae. Thus AbpS connects the interior of the mycelia with the extracellular space and binds cellulose using a unique cellulose-binding module.

Received for publication, December 16, 2002 , and in revised form, May 7, 2003.

^* This work was supported in part by the Sonderforschungsbereich 431. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Universität Osnabrück, FB Biologie/Chemie, Barbarastrae 11, 49069 Osnabrück, Germany. Tel.: 49-541-969-2287; Fax: 49-541-969-2804; E-mail: Stefan.Walter{at}uni-osnabrueck.de.

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