The light organ symbiont Vibrio fischeri possesses two distinct secreted ADP-ribosyltransferases.
AUTOR(ES)
Reich, K A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=178871Documentos Relacionados
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