Effects of copper and tributyltin on stress protein abundance in the rotifer Brachionus plicatilis.

1. Exposure of the rotifer Brachionus plicatilis to elevated temperature resulted in the synthesis of a number of proteins, including a prominent one of 58,000 Da (SP58). 2. This protein is immunologically crossreactive with the 65,000 Da heat shock protein of the moth Heliothis virescens, which is a member of a highly conserved family of mitochondrial proteins. 3. Exposure of rotifers to sublethal doses of CuSO4 leads to a 4-5-fold increase in abundance of SP58, with maximum increase occurring at a dose that is approximately 5% of the LC50 for that compound. 4. A similar response was seen with tributyl tin (TBT). Kinetics of induction were sigmoidal, with induction occurring in the range of 20-30 micrograms/l. 5. No response was observed when rotifers were exposed to aluminum chloride, mercury chloride, pentachlorophenol, sodium arsenite, sodium azide, sodium dodecyl sulfate, or zinc chloride. 6. These results indicate that changes in stress protein abundance may prove useful as a biomarker of exposure to particular toxicants.

[1]  G. Blobel,et al.  70K heat shock related proteins stimulate protein translocation into microsomes , 1988, Nature.

[2]  R. Morimoto,et al.  Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[3]  E. Craig,et al.  The Heat Shock Respons , 1985 .

[4]  R. Hallberg,et al.  A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene , 1988, Molecular and cellular biology.

[5]  R. Guillard,et al.  Culture of Phytoplankton for Feeding Marine Invertebrates , 1975 .

[6]  S. Lindquist.  The heat-shock response. , 1986, Annual review of biochemistry.

[7]  K. Lanks,et al.  Modulators of the eukaryotic heat shock response. , 1986, Experimental Cell Research.

[8]  M. Ashburner,et al.  The induction of gene activity in drosophila by heat shock , 1979, Cell.

[9]  R. Hallberg,et al.  A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila , 1987, Molecular and cellular biology.

[10]  R. Larossa,et al.  Demonstration by genetic suppression of interaction of GroE products with many proteins , 1989, Nature.

[11]  H. Pelham,et al.  Mechanisms of heat-shock gene activation in higher eukaryotes. , 1987, Advances in genetics.

[12]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[13]  H. Bode,et al.  Thermotolerance and synthesis of heat shock proteins: these responses are present in Hydra attenuata but absent in Hydra oligactis. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[14]  D W Nebert,et al.  P450 genes: structure, evolution, and regulation. , 1987, Annual review of biochemistry.

[15]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[16]  Elizabeth A. Craig,et al.  A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides , 1988, Nature.

[17]  G. Lorimer,et al.  Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP , 1989, Nature.

[18]  Roger W. Hendrix,et al.  Homologous plant and bacterial proteins chaperone oligomeric protein assembly , 1988, Nature.

[19]  T. Snell,et al.  Acute toxicity bioassays using rotifers. I. A test for brackish and marine environments with Brachionus plicatilis , 1989 .

[20]  S. Miller.  Association of a sperm-specific protein with the mitochondrial F1F0-ATPase in Heliothis: Implications for sterility of H. virescens × H. subflexa backcross hybrids , 1987 .

[21]  S. Lindquist,et al.  The heat-shock proteins. , 1988, Annual review of genetics.

[22]  C. Harley,et al.  Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen , 1989, Molecular and cellular biology.

[23]  F. Hartl,et al.  Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis , 1989, Nature.

[24]  R. Burdon,et al.  Heat shock and the heat shock proteins. , 1986, The Biochemical journal.

[25]  S. Henikoff,et al.  Localization of RNA from heat-induced polysomes at puff sites in Drosophila melanogaster. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[26]  A. Myers,et al.  Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor , 1989, Nature.