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KMID : 0545120040140051052
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Journal of Microbiology and Biotechnology
2004 Volume.14 No. 5 p.1052 ~ p.1056
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Screening and Characterization of Secretion Signals from Lactococcus lactis ssp. cremoris LM0230
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Jeong DW
Choi YC/Seo JM/Kim JH/Lee JH/Kim KH/Lee HJ
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Abstract
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A secretion signal sequence-selection vector (pGS40) was constructed based on an α-amylase gene lacking a secretion signal and employed for selecting secretion signals from Lactococcus lactis ssp. cremoris LM0230 chromosomal DNA. Six fragments were identified based on their ability to restore α-amylase secretion in E. coli and among these a fragment S405 conferred the highest secretion activity (84%) in E. coli. Meanwhile S407 which conferred poor secretion activity in E. coli was quite active in L. lactis. The results suggested that the efficiency of a secretion signal depended on the host. All six fragments had an open reading frame (ORF) fused to the reporter gene and the potential Shine-Dalgarno (SD) sequence and putative promoter sequences were located upstream of the ORF. Deduced amino acid sequences from the six fragments did not show any homology with known secretion signals. However they contained three distinguished structural features and cleavage sites commonly found among typical secretion signals. The characterized secretion signals could be useful for the construction of foodgrade secretion vectors and gene expression in LAB.
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