Literature DB >> 8706895

Involvement of a single-stranded DNA binding protein, ssCRE-BP/Pur alpha, in morphine dependence.

T Osugi1, Y Ding, H Tanaka, C H Kuo, E Do, Y Irie, N Miki.   

Abstract

We have purified a nuclear protein from mouse cerebella that binds to single-stranded oligo-DNA of cAMP response element and is modulated by morphine treatment. Isolation of the cDNA clone showed that the nuclear protein (ssCRE-BP) was identical to Pur alpha, a DNA binding protein for single-stranded purine-rich sequences that was originally isolated as a replication factor. ssCRE-BP/Pur alpha and mRNA were abundant in the brain. The levels of ssCRE-BP/Pur alpha and the transcript were not changed by chronic morphine treatment, however, the levels of an activator of ssCRE-BP/Pur alpha, which is necessary for the DNA binding, may be modulated by the treatment.

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Year:  1996        PMID: 8706895     DOI: 10.1016/0014-5793(96)00696-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes.

Authors:  Douglas L Theobald; Steve C Schultz
Journal:  EMBO J       Date:  2003-08-15       Impact factor: 11.598

Review 2.  Puralpha: a multifunctional single-stranded DNA- and RNA-binding protein.

Authors:  G L Gallia; E M Johnson; K Khalili
Journal:  Nucleic Acids Res       Date:  2000-09-01       Impact factor: 16.971

  2 in total

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