6533b7d9fe1ef96bd126cd5a
RESEARCH PRODUCT
Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723.
Vladimir OvodHong WangVarpu MarjomäkiMarkku S. Kulomaasubject
CytoplasmBiophysicsBiologyProtein Sorting SignalsBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundBiosynthesisAntibody SpecificityInner membraneMolecular BiologySphingobium chlorophenolicumAlphaproteobacteriachemistry.chemical_classificationAntibodies MonoclonalCell BiologyPeriplasmic spacebiology.organism_classificationSubcellular localizationMolecular biologyImmunohistochemistryPentachlorophenolKineticsEnzymechemistryBiochemistryCytoplasmPeriplasmdescription
Abstract We have studied the subcellular localization of pentachlorophenol 4-monooxygenase (PCP4MO) in Sphingobium chlorophenolicum ATCC 39723 during induction by pentachlorophenol (PCP). Using a monoclonal antibody CL6 specific to the native and recombinant PCP4MO, the enzyme was primarily found soluble as determined by immunoblot and ELISA analyses of cellular fractions. However, the enzyme was observed both in the soluble and membrane-bound forms during induction for 2–4 h, suggesting its translocation out from the cytoplasm. Electron microscopy confirmed that PCP4MO was predominantly present in the cytoplasm at 1 h, whereas at 4 h significant amount was detected also in the membrane and periplasm. After 6 h, the majority of PCP4MO was in the periplasm and only small amount was bound to the inner membrane or present in the cytoplasm. The results indicate that after biosynthesis PCP4MO in S. chlorophenolicum is exported via the inner membrane to the final location in the periplasm.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-12-01 | Biochemical and biophysical research communications |