PMID:7867949
| Citation |
Jekel, M and Wackernagel, W (1995) The periplasmic endonuclease I of Escherichia coli has amino-acid sequence homology to the extracellular DNases of Vibrio cholerae and Aeromonas hydrophila. Gene 154:55-9 |
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| Abstract |
The gene endA, encoding the periplasmic endonuclease I (EndoI) of Escherichia coli, was identified on a cloned chromosomal 1.5-kb HindIII fragment. The nucleotide sequence of the fragment revealed an open reading frame (ORF) coding for a polypeptide of 235 amino acids (aa). The ORF preceeded by a region with two possible promoter sites displays promoter activity when cloned into an expression vector. On the C-terminal side, two sequences with putative transcription termination function are present. The predicted aa sequence suggests the presence of a signal peptide of 22 aa and a signal peptide cleavage site. A cold-shock supernatant from cells harbouring a multicopy endA+ plasmid contained an approx. tenfold higher amount than wild-type cells of the DNA double-strand- and single-strand-cleavage activities characteristic of EndoI. The growth rate and viability of the cells was not affected. The predicted aa sequence of the ORF is 60 and 54% identical to the sequence of extracellular DNases from Vibrio cholerae and Aeromonas hydrophila, respectively. |
| Links | |
| Keywords |
Aeromonas hydrophila/enzymology; Amino Acid Sequence; Bacterial Proteins/chemistry; Base Sequence; Deoxyribonucleases/chemistry; Endodeoxyribonucleases/chemistry; Escherichia coli/enzymology; Membrane Proteins; Molecular Sequence Data; Promoter Regions, Genetic; Sequence Alignment; Sequence Homology, Amino Acid; Terminator Regions, Genetic; Vibrio cholerae/enzymology |
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