作者: Y. S. Lapteva , O. E. Zolova , M. G. Shlyapnikov , I. M. Tsfasman , T. A. Muranova
DOI: 10.1128/AEM.01621-12
关键词:
摘要: Lytic enzymes are the group of hydrolases that break down structural polymers cell walls various microorganisms. In this work, we determined nucleotide sequences Lysobacter sp. strain XL1 alpA and alpB genes, which code for, respectively, secreted lytic endopeptidases L1 (AlpA) L5 (AlpB). silico analysis their amino acid showed these to be homologous proteins synthesized as precursors similar in organization: mature enzyme sequence is preceded by an N-terminal signal peptide a pro region. On basis phylogenetic analysis, AlpA AlpB were assigned S1E family [clan PA(S)] serine peptidases. Expression open reading frames (ORFs) Escherichia coli confirmed they for functionally active enzymes. Each ORF was predicted have Shine-Dalgarno located at canonical distance from start codon potential Rho-independent transcription terminator immediately after stop codon. The mRNAs experimentally found monocistronic; points both mRNAs. synthesis shown occur predominantly late logarithmic growth phase. amount mRNA cells much higher, correlates with greater production endopeptidase than L5.