Cloning, Sequencing, and Characterization of Two Clustered Cellulase-Encoding Genes, celS1 and celS2, from Streptomyces viridosporus T7A and their Expression in Escherichia coli.
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A recombinant clone, pBLP, containing a 4.1kb fragment of <I>Streptomyces viridosporus</I> T7A chromosomal DNA was shown to confer endoglucanase activity in <I>Escherichia coli</I> cells. Further subcloning and sequence analysis revealed two co-transcribed Open Reading Frames (ORF) with high sequence similarities to other <I>Streptomyces</I> endoglucanase-encoding genes. A signal peptide, a catalytic domain and cellulose binding domain were identified within ORF1 (<I>celS1</I>). The amino acid sequence of ORF2 (<I>celS2</I>) showed similarity with cellulose binding protein (p40) of <I>Streptomyces halstedii</I>. The hydrophobic analysis of CelSl revealed that it belongs to the family H cellu-lase catalytic domain. The rare TTA codon encoding leucine was found in the signal sequence of both the cellu-lase ORFs, indicating translational dependence on the <I>bldA</I> gene product, a cognate tRNA responsible for translating the TTA codons. The presence of 14 bp inverted repeats in the 5'-end of these genes, was consistent with the highly conserved positive regulatory structure found in other endoglucanase genes.
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