The light organ symbiont Vibrio fischeri possesses two distinct secreted ADP-ribosyltransferases.
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.
Reich
K A
KA
Department of Microbiology and Immunology, Stanford University School of Medicine, California 94305, USA.
Biegel
T
T
Schoolnik
G K
GK
D001426:Bacterial Proteins; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000235:genetics; D008163:Luminescent Measurements; D008970:Molecular Weight; D009154:Mutation; D010430:Pentosyltransferases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis; D013559:Symbiosis; D014733:Vibrio / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D010430:Pentosyltransferases; C097620:hvn protein, Vibrio fischeri