Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli.

@article{Ehlert1995CloningAE,
  title={Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli.},
  author={K Ehlert and J. - V. H{\"o}ltje and Markus F. Templin},
  journal={Molecular microbiology},
  year={1995},
  volume={16 4},
  pages={
          761-8
        }
}
On the basis of the published N-terminal amino acid sequence of the soluble lytic transglycosylase 35 (Slt35) of Escherichia coli, an open reading frame (ORF) was cloned from the 60.8 min region of the E. coli chromosome. The nucleotide sequence of the ORF, containing a putative lipoprotein-processing site, was shown by [3H]-palmitate labelling to encode a lipoprotein with an apparent molecular mass of 36 kDa. A larger protein, presumably the prolipoprotein form, accumulated in the presence of… CONTINUE READING
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