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Volume 271, Number 43,
Issue of October 25, 1996
pp. 26914-26923
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Zebrafish Pax9 Encodes Two Proteins with Distinct
C-terminal Transactivating Domains of Different Potency Negatively
Regulated by Adjacent N-terminal Sequences
(Received for publication, November 28, 1995, and in revised form, July 3, 1996)
Svanhild
Nornes
,
Ingvild
Mikkola
,
Stefan
Krauss
,
Madjid
Delghandi
,
Maria
Perander
and
Terje
Johansen
From the Departments of Biochemistry and
Molecular Genetics, Institute of Medical Biology, University of
Tromsø, 9037 Tromsø, Norway
We describe the isolation of cDNA clones for
zebrafish Pax9. Pax9 expression was initiated at the end of
the segmentation period in mesenchymal sclerotome cells on both sides
of the notochord similarly to the corresponding mouse and chick genes.
Two transcripts, Pax9a and -b, are generated by
alternative splicing. The gene contains 4 exons with exon 3 being
included in the Pax9a transcript and spliced out in the
Pax9b transcript. The Pax9a and -b proteins are identical
for 212 amino acids from the N terminus but contain distinct C-terminal
regions of 131 and 58 amino acids, respectively. The paired domain of
Pax9 displayed a binding-site specificity distinct from Pax6 but
similar to Pax1 and -2. Both Pax9a and -b activated a promoter
containing a paired domain binding site. However, this activation was
observed when low amounts of Pax9 expression vectors were used. Higher
amounts led to a sharp decrease in the activation and even turned into
repression. Both the distinct C-terminal regions of Pax9a and -b
harbored transcriptional activating domains of different potency not
revealed in the context of the full-length proteins due to a negative
influence of the N-terminal region including the paired domain.

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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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