title: Wide distribution of the cysteine string proteins in Drosophila tissues revealed by targeted mutagenesis.
abstract: The "cysteine string protein" (CSP) genes of higher eukaryotes code for a novel family of proteins characterized by a "J" domain and an unusual cysteine-rich region. Previous studies had localized the proteins in neuropil and synaptic terminals of larval and adult Drosophila and linked the temperature-sensitive paralysis of the mutants described here to conditional failure of synaptic transmission. We now use the null mutants as negative controls in order to reliably detect even low concentrations of CSPs by immunohistochemistry, employing three monoclonal antibodies. In wild-type flies high levels of cysteine string proteins are found not only in apparently all synaptic terminals of the embryonic, larval, and adult nervous systems, but also in the "tall cells" of the cardia, in the follicle cells of the ovary, in specific structures of the female spermatheca, and in the male testis and ejaculatory bulb. In addition, low levels of CSPs appear to be present in all tissues examined, including neuronal perikarya, axons, muscles, Malpighian tubules, and salivary glands. Western blots of isolated tissues demonstrate that of the four isoforms expressed in heads only the largest is found in non-neural organs. The wide expression of CSPs suggests that at least some of the various phenotypes of the null mutants observed at permissive temperatures, such as delayed development, short adult lifespan, modified electroretinogram, and optomotor behavior, may be caused by the lack of CSPs outside synaptic terminals.
authors.affiliation: Th.-Boveri-Institut für Biowissenschaften, Lehrstuhl für Genetik, Am Hubland, D-97074 Würzburg, Germany.
authors.forename: K K
authors.initials: KK
authors.lastname: Eberle
authors.forename: K E
authors.initials: KE
authors.lastname: Zinsmaier
authors.forename: S
authors.initials: S
authors.lastname: Buchner
authors.forename: M
authors.initials: M
authors.lastname: Gruhn
authors.forename: M
authors.initials: M
authors.lastname: Jenni
authors.forename: C
authors.initials: C
authors.lastname: Arnold
authors.forename: C
authors.initials: C
authors.lastname: Leibold
authors.forename: D
authors.initials: D
authors.lastname: Reisch
authors.forename: N
authors.initials: N
authors.lastname: Walter
authors.forename: E
authors.initials: E
authors.lastname: Hafen
authors.forename: A
authors.initials: A
authors.lastname: Hofbauer
authors.forename: G O
authors.initials: GO
authors.lastname: Pflugfelder
authors.forename: E
authors.initials: E
authors.lastname: Buchner
mesh_terms: D000367:Age Factors; D000818:Animals; D015153:Blotting, Western; D018833:Chaperonins / Q000737:chemistry / Q000235:genetics; D003001:Cloning, Molecular; D004331:Drosophila melanogaster / Q000235:genetics*; D004596:Electroretinography; D005089:Exocytosis / Q000502:physiology; D005260:Female; D018507:Gene Expression Regulation, Developmental; D050956:HSP40 Heat-Shock Proteins; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics*; D007814:Larva / Q000737:chemistry / Q000502:physiology; D008297:Male; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000235:genetics; D009420:Nervous System / Q000737:chemistry / Q000254:growth & development; D010641:Phenotype; D017729:Presynaptic Terminals / Q000737:chemistry; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013696:Temperature
chemical_list: D050956:HSP40 Heat-Shock Proteins; D019476:Insect Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C088460:cysteine string protein; D018833:Chaperonins