Luciferases are unique enzymes in being capable of emitting visible light a
s one of the end-products of their catalysis. Both procaryotic and eucaryot
ic organisms exist that emit light, and the luciferases from these organism
s differ considerably in size as well as chemistry of catalysis. Two main,
i.e. most studied groups, are the bacterial luciferases of e.g. Vibrio fish
eri, Vibrio harveyi, and Photorhabdus luminescens, responding to FMNH2, lon
g-chain aldehyde and molecular oxygen and the insect luciferases of the fir
eflies Photinus pyralis and Luciola minengrelica or click beetle Pyrophorus
plagiophthalamus, responding to ATP, luciferin and molecular oxygen. An em
erging amount of 'new' luciferases from shrimps, fish, jelly fish and overa
ll from marine origin, are finding their way to biotechnological applicatio
ns. The common feature of these is their ability to produce light within th
e visible region of the spectrum, i.e. between 450 nm (blue) and 630 nm (re
d). In this short review, we discuss some of the recent advances on fusion
proteins of eucaryotic luciferases and their applications. Special emphasis
is placed on a streptavidin-luciferase fusion protein produced by insect c
ells using the baculovirus expression system. (C) 1999 Elsevier Science B.V
. All rights reserved.