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KMID : 1007519970060040304
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Food Science and Biotechnology
1997 Volume.6 No. 4 p.304 ~ p.308
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Cloning and Sequencing of an aprL gene of Bacillus licheniformis NS70 encoding an Alkaline Protease
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OH, TAE KWANG
Nam, Hee Sop/Lee, Hyung Jae/Chae, Keon Sang/Yang, Moon Sik/Hwang, Hyun Ah/Kim, Jong Hwa
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Abstract
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Three independently amplified DNA fragments of an aprL gene of Bacillus licheniformis NS70 encoding an alkaline protease were obtained by polymerase chain reaction (PCR) and their nucleotide sequences, which is 1,184 bp in total, were determined completely in both directions to find out the correct sequence of the gene. The determined nucleotide sequence indicated that there is an 1,137 bp open reading frame (ORF) possibly encoding a 379 amino acid polypeptide. A putative Shine-Dalgarno (SD) sequence was found 8 bp upstream from the translation initiation codon, ATG. The aprL gene showed an identity with that of B. licheniformis keratinase (99%), or subtilisin Carlsberg (98%) in the nucleotide sequence. The deduced amino acid sequence revealed a putative N-terminal signal peptide of 29 amino acid residues and a pro-peptide of 76 amino acid residues followed by the 274 amino acid mature protein. The AprL ORF had a codon bias index (CBI) of 0.27 which suggested that it may not be translated in a large amount in E. coli, and showed 98% similarity with subtilisin Carlsberg in the amino acid sequence.
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KEYWORD
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