The bovine tyrosine hydroxylase gene associates in vitro with the nuclear matrix by its first intron sequence

• Autorzy: Lenartowski R. , Grzybowski T. , Miscicka-Sliwka D. , Wojciechowski W. , Goc A.
• Języki publikacji: EN

Abstrakty

EN

Recently we have shown that in vitro binding of the proximal part of the human tyro­sine hydroxylase gene to the nuclear matrix is correlated with its transcriptional activ­ity. The strongest binding potential was predicted by computing for the first intron se­quence (Lenartowski & Goc, 2002, Neurosci Lett.; 330: 151-154). In this study a 16 kb fragment of the bovine genomic DNA containing the tyrosine hydroxylase gene was investigated for its affinity to the nuclear matrix. Only a 950 bp fragment encod­ing the distal part of the first intron, second exon and a few nucleotides of the second intron bound to the nuclear matrix. The binding was independent of the tissue-specific tyrosine hydroxylase gene activation. The fragment was subcloned and sequenced. Computer search pointed to one potential intronic matrix attachment region with two AP1-like sites embedded in the sequence. We conclude that even if the position of the matrix binding region is conserved among the tyrosine hydroxylase genes in mam­mals, its tissue specificity and/or function is not preserved or is achieved by different mechanisms.

Słowa kluczowe

EN

gene; tissue specificity; nuclear matrix; in vitro; tyrosine hydroxylase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.865-873,fig.

Twórcy

autor

Lenartowski R.

• N.Copernicus University, I.Gagarina 9, 87-100 Torun, Poland

autor

Grzybowski T.

autor

Miscicka-Sliwka D.

autor

Wojciechowski W.

autor

Goc A.

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