Ca. Callahan et Jb. Thomas, TAU-BETA-GALACTOSIDASE, AN AXON-TARGETED FUSION PROTEIN, Proceedings of the National Academy of Sciences of the United Statesof America, 91(13), 1994, pp. 5972-5976
The most commonly used enzymatic reporter molecule, Escherichia coli b
eta-galactosidase (beta-gal; beta-D-galactoside galactohydrolase, EC 3
.2.1.23), fails to readily diffuse into axons; consequently, the morph
ologies of beta gal-labeled neurons cannot directly be determined. For
analysis of neuronal pathfinding and synaptic connectivity, this info
rmation is essential. We have constructed an axon-targeted beta-gal re
porter by fusing the cDNA encoding the bovine microtubule-binding prot
ein, tau, to lacZ, the E. coli gene encoding beta-gal. This reporter l
abels cell bodies and axons when expressed by developing and adult Dro
sophila neurons. It also reveals the entire cellular extent of nonneur
onal cells such as muscle fibers and glia. To generate neuronal marker
s for studies of Drosophila neural development, we constructed a tau-b
eta-gal enhancer-trap transposon. From 1500 independent lines generate
d by mobilization of this transposon, we have isolated a set of useful
markers for specific subsets of neurons, glia, and muscles. Since the
tau cDNA-lacZ reporter utilizes bovine tau, it may also effectively t
arget beta-gal in vertebrate neurons and prove to be a useful reagent
for the analysis of vertebrate nervous systems.