Tau-β-Galactosidase, an Axon-Targeted Fusion Protein

The most commonly used enzymatic reporter molecule, Escherichia coli β-galactosidase (β-gal; β-D-galactoside galactohydrolase, EC 3.2.1.23), fails to readily diffuse into axons; consequently, the morphologies of β-gal-labeled neurons cannot directly be determined. For analysis of neuronal pathfindin...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1994-06, Vol.91 (13), p.5972-5976
Hauptverfasser: Callahan, Christopher A., Thomas, John B.
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container_title Proceedings of the National Academy of Sciences - PNAS
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Thomas, John B.
description The most commonly used enzymatic reporter molecule, Escherichia coli β-galactosidase (β-gal; β-D-galactoside galactohydrolase, EC 3.2.1.23), fails to readily diffuse into axons; consequently, the morphologies of β-gal-labeled neurons cannot directly be determined. For analysis of neuronal pathfinding and synaptic connectivity, this information is essential. We have constructed an axon-targeted β-gal reporter by fusing the cDNA encoding the bovine microtubule-binding protein, tau, to lacZ, the E. coli gene encoding β-gal. This reporter labels cell bodies and axons when expressed by developing and adult Drosophila neurons. It also reveals the entire cellular extent of nonneuronal cells such as muscle fibers and glia. To generate neuronal markers for studies of Drosophila neural development, we constructed a tau-β-gal enhancer-trap transposon. From 1500 independent lines generated 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 target β-gal in vertebrate neurons and prove to be a useful reagent for the analysis of vertebrate nervous systems.
doi_str_mv 10.1073/pnas.91.13.5972
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Thomas, John B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c559t-2b5ffe7dcec813125d52086017e9c615b792b1f0468239a0bd345bfbb943fead3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Axons</topic><topic>Axons - physiology</topic><topic>beta-Galactosidase - analysis</topic><topic>beta-Galactosidase - biosynthesis</topic><topic>Cattle</topic><topic>Central nervous system</topic><topic>Drosophila</topic><topic>Drosophila - embryology</topic><topic>Drosophila - physiology</topic><topic>Embryo, Nonmammalian - physiology</topic><topic>Embryos</topic><topic>Escherichia coli - enzymology</topic><topic>Immunohistochemistry</topic><topic>Motor neurons</topic><topic>Neuroglia</topic><topic>Neurons</topic><topic>Neurons - metabolism</topic><topic>Neurons - physiology</topic><topic>Organ Specificity</topic><topic>Recombinant Fusion Proteins - analysis</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Restriction Mapping</topic><topic>tau Proteins - analysis</topic><topic>tau Proteins - biosynthesis</topic><topic>Ungulates</topic><topic>Vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Callahan, Christopher A.</creatorcontrib><creatorcontrib>Thomas, John B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Callahan, Christopher A.</au><au>Thomas, John B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tau-β-Galactosidase, an Axon-Targeted Fusion Protein</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-06-21</date><risdate>1994</risdate><volume>91</volume><issue>13</issue><spage>5972</spage><epage>5976</epage><pages>5972-5976</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The most commonly used enzymatic reporter molecule, Escherichia coli β-galactosidase (β-gal; 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subjects Animals
Antibodies
Axons
Axons - physiology
beta-Galactosidase - analysis
beta-Galactosidase - biosynthesis
Cattle
Central nervous system
Drosophila
Drosophila - embryology
Drosophila - physiology
Embryo, Nonmammalian - physiology
Embryos
Escherichia coli - enzymology
Immunohistochemistry
Motor neurons
Neuroglia
Neurons
Neurons - metabolism
Neurons - physiology
Organ Specificity
Recombinant Fusion Proteins - analysis
Recombinant Fusion Proteins - biosynthesis
Restriction Mapping
tau Proteins - analysis
tau Proteins - biosynthesis
Ungulates
Vertebrates
title Tau-β-Galactosidase, an Axon-Targeted Fusion Protein
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