Evidence for the subcellular localization and specificity of chlordane inhibition in the marine bacterium Aeromonas proteolytica.
Sublethal levels (10 to 100 micrograms/ml) of the chlorinated insecticide chlordane (1,2,4,5,6,7,8,8-octachloro-3a,4,7,7a-tetrahydro-4,7-methanoindan) were introduced into the growth medium of the marine bacterium, Aeromonas proteolytica. Chlordane inhibited the synthesis of an extracellular endopeptidase by almost 40% but exhibited no such inhibition of the extracellular aminopeptidase also produced during the growth cycle. Studied with 14C-labeled chlordane demonstrated that the insecticide was not biologically degraded under the test conditions used and that up to 75% of the recoverable chlordane was cell associated within 48 h. Studied with uniformly labeled L[14C]valine and [2-14C]uracil established that neither the transport nor the incorporation of these protein and ribonucleic acid precursors was inhibited by chlordane. Separation of the membrane fractions using isopycnic centrifugation localized 14C-labeled chlordane in the cytoplasmic membrane. Also, chlordane inhibited the membrane-bound adenosine 5'-triphosphatase while the soluble (released) form of this enzyme remained unaffected. These data indicate that chlordane resides in the cytoplasmic membrane and may cause specific alterations in membrane-associated activities.
D000251:Adenosine Triphosphatases / Q000096:biosynthesis; D000333:Aeromonas / Q000187:drug effects* / Q000378:metabolism; D000626:Aminopeptidases / Q000096:biosynthesis; D002462:Cell Membrane / Q000378:metabolism; D002474:Cell-Free System; D002706:Chlordan / Q000378:metabolism / Q000494:pharmacology*; D010450:Endopeptidases / Q000096:biosynthesis; D012623:Seawater; D014871:Water Microbiology; D014877:Water Pollution, Chemical
D002706:Chlordan; D010450:Endopeptidases; D000626:Aminopeptidases; D000251:Adenosine Triphosphatases