Skip to main content
Log in

Immunofluorescence localization of a small heat shock protein (hsp 23) in salivary gland cells of Drosophila melanogaster

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

An aggregate present in cell-free extracts of Drosophila melanogaster tissue culture cells, sedimenting at 20 to 30S, contains hsps 23, 26 and 27. Hsp 23 was purified from this aggregate and a monospecific antibody was raised against it. Immunofluorescence microscopy showed the presence of hsp 23 preferentially in nuclei after heat shock, while on return to 25° C, hsp 23 was reduced in nuclei and increased in the cytoplasm. Thus the immunofluorescence observations reported here unambignously confirm for hsp 23 earlier reports that heat shock proteins are mainly found in nuclei after heat shock and that upon return to 25° C, they move to the cytoplasm.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

NP-40:

Nonidet P40

PMSF:

Phenylmethylsulfonyl-fluoride

SDS:

Sodium dodecyl sulfate

EDTA:

Ethylene diamine tetraacetic acid

TCA:

Trichloroacetic acid. hsp 22, hsp 23 etc.: heat shock proteins of 22,000, 23,000 daltons etc. molecular weight

References

  • Arrigo AP (1981) Study of the interaction of heat shock proteins in the chromatin of D. melanogaster tissue culture cells. Mol Gen Genet submitted

  • Arrigo AP (1980) Investigation of the function of the heat shock proteins in Drosophila melanogaster tissue culture cells. Mol Gen Genet 178:517–524

    Google Scholar 

  • Arrigo AP, Fakan S, Tissières A (1980) Localization of the heat shock-induced proteins in Drosophila melanogaster tissue culture cells. Dev Biol 78:86–103

    Google Scholar 

  • Ashwell G (1957) Colorimetric analysis of sugars. In: Colowick SP, Kaplan NO (eds) Methods of enzymology, vol III. Academic Press, New York, pp 87–90

    Google Scholar 

  • Burton K (1956) A study of the conditions and mechanisms of the diphenylamin reaction for the colorimetric estimation of deoxyribonucleic acid. Biochemistry 62:315–323

    Google Scholar 

  • Echallier G, Ohanessian A (1970) In vitro culture of Drosophila melanogaster embryonic cells. In Vitro 6:162–171

    Google Scholar 

  • Kelly PM, Schlessinger MJ (1978) The effect of amino acid analogues and heat shock on gene expression in chicken embryos fibroblasts. Cell 15:1277–1286

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Google Scholar 

  • Lewis M, Helmsing PJ, Ashburner M (1975) Parallel changes in puffing activity and pattern of protein synthesis in salivary glands of Drosophila. Proc Natl Acad Sci USA 72:3604–3608

    Google Scholar 

  • Lowry O, Rosenbrough A, Farr A, Randall R (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    Google Scholar 

  • McKenzie SL, Henikoff S, Meselson M (1975) Localization of heat-induced polyribosomal RNA. Proc Natl Acad Sci USA 72:1117–1121

    Google Scholar 

  • Malnoe P, Rochaix J-D, Chua NH, Spahr P-F (1979) Characterization of the gene and messenger RNA of the large subunit of ribulose 1,5-diphosphate carboxylase in Chlamydomonas reinhardii. J Mol Biol 133:417–434

    Google Scholar 

  • Miller MJ, Nguyen-Huu Xuong, Geiduschek EP (1979) A response of protein synthesis to temperature shift in yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA 76:5222–5225

    Google Scholar 

  • Mirault M-E, Goldschmidt-Clermont M, Moran L, Arrigo A-P, Tissières A (1978) The effect of heat shock on gene expression in Drosophila melanogaster. Cold Spring Harbor Symp Quant Biol 42:819–827

    Google Scholar 

  • Mitchell HK, Lipps LS (1975) Rapidyl labeled proteins on the salivary gland chromosomes of Drosophila melanogaster. Biochem Genet 13:585–602

    Google Scholar 

  • Peacock A, Dingman C (1968) Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. Biochemistry 7:668–674

    Google Scholar 

  • Preobrazhensky AA, Spirin AS (1978) Informosomes and their protein components: the present state of knowledge. In: Cohn WE (ed) Progress in nuclear acid research and molecular biology, vol 21. Academic Press, New York, pp 1–37

    Google Scholar 

  • Ritossa FM (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18:571–573

    Google Scholar 

  • Ritossa FM (1964) Behavior of RNA and DNA synthesis at the puff level in salivary gland chromosomes of Drosophila. Exp Cell Res 36:515–523

    Google Scholar 

  • Tissières A, Mitchell HK, Tracy UM (1974) Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 84:389–398

    Google Scholar 

  • Velasquez JM, DiDomenico BJ, Lindquist S (1980) Intracellular localization of heat shock proteins in Drosophila. Cell 20:679–689

    Google Scholar 

  • Voellmy R, Goldschmidt-Clermont M, Southgate R, Tissières A, Levis R, Gehring W (1981) A DNA segment isolated from chromosomal site 67B in D. melanogaster contains four closely linked heat shock genes. Cell 23:261–270

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Communicated by W. Gehring

Rights and permissions

Reprints and permissions

About this article

Cite this article

Arrigo, A.P., Ahmad-Zadeh, C. Immunofluorescence localization of a small heat shock protein (hsp 23) in salivary gland cells of Drosophila melanogaster . Molec. Gen. Genet. 184, 73–79 (1981). https://doi.org/10.1007/BF00271198

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00271198

Keywords

Navigation