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. 1996 Jan;178(1):209–215. doi: 10.1128/jb.178.1.209-215.1996

Halovibrin, secreted from the light organ symbiont Vibrio fischeri, is a member of a new class of ADP-ribosyltransferases.

K A Reich 1, G K Schoolnik 1
PMCID: PMC177641  PMID: 8550419

Abstract

The purification, cloning, and deduced amino acid sequence of an ADP-ribosyltransferase secreted from the marine bacterium Vibrio fischeri (V. fischeri ADP-r) is described. This enzyme was purified from culture supernatant, and partial amino acid sequence obtained from the purified protein was used to design a degenerate oligonucleotide probe that was used to clone a cross-hybridizing DNA fragment from V. fischeri genomic DNA. Recombinant Escherichia coli clones harboring this fragment possessed ADP-ribosyltransferase activity. The DNA fragment was sequenced, and deletion analysis localized the ADP-ribosyltransferase activity to one of the three possible open reading frames in the fragment; the deduced amino acid sequence from this open reading frame matched the amino acid sequence obtained from the purified protein. V. fischeri ADP-r has no significant homology (DNA or amino acid) with other known ADP-ribosyltransferases. This enzyme appears to require neither proteolytic cleavage nor a reducing agent for enzymatic activity. The cloned gene is expressed but not secreted in E. coli; however, it is secreted from a heterologous marine Vibrio species. We have named this enzyme halovibrin.

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Selected References

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