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Publication : DNA binding and transactivating properties of the paired and homeobox protein Pax4.

First Author  Kalousová A Year  1999
Journal  Biochem Biophys Res Commun Volume  259
Issue  3 Pages  510-8
PubMed ID  10364449 Mgi Jnum  J:55703
Mgi Id  MGI:1339227 Doi  10.1006/bbrc.1999.0809
Citation  Kalousova A, et al. (1999) DNA binding and transactivating properties of the paired and homeobox protein Pax4. Biochem Biophys Res Commun 259(3):510-8
abstractText  Transcription factors Pax-4 and Pax-6 are known to be key regulators of pancreatic cell differentiation and development. We report on the cloning of a mouse Pax-4 gene, which contains 10 exons, spanning a 4. 7-kbp region. The gene-targeting experiments revealed that Pax-4 and Pax-6 cannot substitute for each other in tissue with overlapping expression of both genes. We identified DNA-binding specificities of Pax-4 paired domain and paired-type homeodomain. Despite the different Pax-4 amino acid residues in positions responsible for Pax-6 paired-domain specificity, the DNA-binding specificities of Pax-4 and Pax-6 are similar. The Pax-4 homeodomain was shown to preferentially dimerize on DNA sequences consisting of an inverted TAAT motif, separated by 4-nucleotide spacing. The Pax-4 transactivation domain was localized within its C-terminal region, which transactivated GAL-based reporter 2.5-fold less than the C-terminal region of Pax-6. We believe that Pax-4 can act as a Pax-6 repressor, due to the competition for binding sites and lower transactivation potential of Pax-4. Copyright 1999 Academic Press.
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