Gary Schoolnik

Publication Details

  • The light organ symbiont Vibrio fischeri possesses two distinct secreted ADP-ribosyltransferases JOURNAL OF BACTERIOLOGY Reich, K. A., Biegel, T., SCHOOLNIK, G. K. 1997; 179 (5): 1591-1597


    We have previously described the purification, cloning, and initial characterization of a secreted ADP-ribosyltransferase, halovibrin (gene designation hvn), from the luminescent light organ symbiont Vibrio fischeri. This report describes a strategy for overexpression of halovibrin, the production and refinement of antihalo-vibrin antisera, and the molecular biological construction of a V. fischeri halovibrin null strain. Biochemical analysis of this mutant revealed that V. fischeri hvn null still possessed ADP-ribosyltransferase activity and that this activity is immunologically, genetically, and structurally distinct from the previously described enzyme. This unusual finding, of two ADP-ribosyltransferase enzymes produced by a microorganism, is complemented by the details of the purification to apparent homogeneity and in vitro regulation of this new protein, halovibrin-beta.

    View details for Web of Science ID A1997WP41500022

    View details for PubMedID 9045818

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