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  • 1990-1994  (2)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Galactose-induced puffing changes inChironomus thummi Balbiani rings and their dependence on protein synthesis (1990)
    Springer
    Chromosoma 99 (1990), S. 61-70 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract InChironomus thummi, puffing changes induced by galactose treatment (sugar effect) are restricted to the Br1/BR2 (Balbiani ring) system. No obvious induction of additional BRs such as BR6 inCamptochironomus pallidivittatus occurs. The response to feeding galactose (or other sugars), i.e. BR2 regression and concomitant BR1 activation, usually takes 24–48 h but can be accelerated somewhat by the application of two 6 h galactose treatments separated by an 18 h interval without sugar. In the “special cells” composing the lateral lobe of the salivary gland galactose causes regression on BR2 without concomitant BR1 activation which, however, appears delayed. The autonomous collapse of BR2 therefore could be considered as the primary effect of galactose at the puffing level. On the other hand, inhibition experiments performed with cycloheximide (CHM) emphasize the relevance of translational events in the control of the sugar effect. At highly inhibitory doses, CHM prevents the induction or causes reactivation of galactose-repressed BR2, suggesting that both induction and maintenance of the galactose effect are dependent on newly synthesized proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01737290
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunoelectron microscope localization of Mr 90000 heat shock protein and Mr 70000 heat shock cognate protein in the salivary glands of Chironomus thummi (1992)
    Springer
    Chromosoma 102 (1992), S. 50-59 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The Mr 90000 heat shock protein (hsp 90) and one of the Mr 70000 heat shock cognate proteins (hsc 70) were localized by immunoelectron microscopy in salavary gland cells of normal and heat-shocked larvae of Chironomus thummi using polyclonal antibodies raised against Drosophila proteins. Immunoblotting after separation of proteins by gel electrophoresis shows that these antibodies cross-react with the corresponding proteins of Chironomus. Hsp 90 was localized both in the cytoplasm and in the nucleus, where it is associated with intrachromosomal and extrachromosomal ribonucleoprotein (RNP) fibrils, as well as with the peripheral region of compact chromatin. After heat shock the concentration of hsp 90 increases in the nucleus. This increase is prevented by actinomycin D administration during the heat shock. Hsp 90 is associated with the chromatin of puffs repressed by heat shock and with the RNP fibrils of actively transcribing heat shock puffs. Hsc 70 is mainly found in RNP fibrils and in the periphery of compact chromatin. During heat shock the concentration of hsc 70 decreases in the cytoplasm while it becomes more abundant in association with chromatin and intrachromosomal and extrachromosomal RNP fibrils. These results suggest a translocation of the existing protein from the cytoplasm toward the nucleus. They are supported by observations of the effect of heat shock carried out in the presence of actinomycin D.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352290
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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