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Phenobarbitone-mediated translocation of the cytosolic proteins interacting with the 5'-proximal region of rat liver CYP2B1/B2 gene into the nucleus.

Authors
  • Samudre, Kalpana R
  • Mani, S A
  • Vathsala, P G
  • Rangarajan, P N
  • Padmanaban, G
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Mar 29, 2002
Volume
292
Issue
2
Pages
312–317
Identifiers
PMID: 11906163
Source
Medline
License
Unknown

Abstract

The positive element (PE) (-69 to -98 bp) within the 5'-proximal region of the CYP2B1/B2 gene (+1 to -179 bp) of rat liver is essential for phenobarbitone (PB) response and gives a single major complex with the rat liver cytosol in gel shift analysis. This complex corresponds to complex I (top) of the three complexes given by the nuclear extracts. PB treatment of rats leads to a decrease in complex I formation with the cytosol and PE and an increase in the same with the nuclear extract in gel shift analysis. Both the changes are counteracted by simultaneous okadaic acid administration. The nuclear protein giving rise to complex I has been isolated and has an M(r) of 26 kDa. The cytosolic counterpart consists of two species, 26 and 28 kDa, as revealed by Southwestern blot analysis using labeled PE. It is concluded that PB treatment leads to the translocation accompanied by processing of the cytosolic protein species into the nucleus that requires protein dephosphorylation. It is suggested that PB may exert a global regulation on the transcription of many genes by modulating the phosphorylation status of different protein factors involved in transcriptional regulation.

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