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The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB

Universität Osnabrück, FB Biologie/Chemie, Barbarastraße 11, D-49069 Osnabrück, Germany

Correspondence
Darío Ortiz de Orué Lucana
ortiz{at}biologie.uni-osnabrueck.de
Hildgund Schrempf
schrempf{at}biologie.uni-osnabrueck.de

The Gram-positive soil bacterium and cellulose degrader Streptomyces reticuli synthesizes the mycelium-associated enzyme CpeB, which displays haem-dependent catalase and peroxidase activity, as well as haem-independent manganese-peroxidase activity. Downstream of the cpeB gene, a so far unknown gene was identified. The new gene and its mutated derivatives were cloned in Escherichia coli as well as in Streptomyces lividans and a gene-disruption mutant within the chromosome of the original S. reticuli host was constructed, comparative physiological, biochemical and immunological studies then allowed the deduction of the following characteristics of the novel gene product. (i) The protein was found extracellularly; the substitution of twin arginines within the signal peptide abolished its secretion. (ii) The highly purified protein interacted specifically with haem and hence was designated HbpS (haem-binding protein of Streptomyces). (iii) HbpS contained three histidine residues surrounded by hydrophobic amino acids; one of them was located within the motif LX₃THLX₁₀AA, which is related to the motif within the yeast cytochrome c peroxidase LX₂THLX₁₀AA whose histidine residue interacts with haem. (iv) The addition of haemin (Fe³⁺ oxidized form of haem) to the Streptomyces cultures led to enhanced levels of HbpS which correlated with increased haemin-resistance. (v) The presence of HbpS increased synthesis of the highly active catalase-peroxidase CpeB containing haem. In this process HbpS could act as a chaperone that binds haem and then delivers it to the mycelium-associated CpeB; HbpS could also interact with membrane-associated proteins involved in a signal transduction cascade regulating the expression of cpeB. (vi) HbpS shared varying degrees of amino acid identities with bacterial proteins of so far unknown function. This report contributes to the elucidation of the biological function of these proteins.

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