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Arch Microbiol. 2008 Aug;190(2):119-27. doi: 10.1007/s00203-008-0373-7. Epub 2008 Apr 26.

Characteristics of the surface-located carbohydrate-binding protein CbpC from Streptomyces coelicolor A32.

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  • 1FB Biologie/Chemie, Universität Osnabrück, Barbarastr 11, 49069 Osnabrück, Germany. stefan.walter@uni-osnabrueck.de

Abstract

Streptomyces coelicolor A32 produces a 35.6-kDa carbohydrate-binding protein (named CbpC) in the presence of cellobiose, cellulose or chitin as sole carbon source. The protein was found secreted (a typical signal sequence was present at the N-terminus) and linked to the peptidoglycan layer of the mycelia. At its C-terminal end a putative cell-wall sorting signal was identified, consisting of (1) Streptomyces specific recognition site for a transpeptidase (LAETG instead of generic LPXTP consensus), (2) a hydrophobic region and (3) a tail of positively charged residues. The deletion of this sorting signal abolished the cell-wall attachment because the resulting CbpC-form was found extracellular. After purification this protein was shown to interact strongly with crystalline cellulose; different crystalline chitin-forms were recognised moderately and chitosan not. As demonstrated by analysing further truncated CbpC-forms a glycine-aspartate/serine rich region, which separates the carbohydrate-binding module from the sorting signal, plays an important role in protein stability.

[PubMed - indexed for MEDLINE]
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