Abstract
A gene coding for xylanase (endo-1,4-β-d-xylan xylanohydrolase, EC 3.2.1.8) from Bacillus subtilis PAP115 has been isolated and its complete nucleotide sequence determined. Starting from an ATG initiator codon, an open reading frame coding for 213 amino acids was found. The N terminus of the processed enzyme as expressed in Escherichia coli was located by amino acid sequence analysis. The amino acid analysis and apparent molecular weight (22,000) of the expressed enzyme were consistent with the translated nucleotide sequence. A proposed 28-residue signal sequence of the enzyme shows features comparable with other Bacillus signal sequences, namely a negatively charged region close to methionine followed by a long hydrophobic string. The coding sequence is preceded by a possible ribosome binding site and, further upstream, by potential transcription initiation signals. When the xylanase amino acid sequence was compared to a xylanase from B. pumilus, strong evidence for homology was found, with over 50% identities in the processed enzymes.
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