Nucleic Acids Research, Vol 26, Issue 16 3800-3805, Copyright © 1998 by Oxford University Press
E Serra, K Zemzoumi, A di Silvio, R Mantovani, V Lardans and C Dissous
The CCAAT-binding protein NF-Y is involved in the regulation of a variety
of eukaryotic genes and is formed in higher eukaryotes by three subunits
NF-YA/B/C. We have characterized NF-Y of the trematode parasite Schistosoma
mansoni and studied the structure and the function of the SMNF-YA subunit.
In this work, we present the cloning and sequence analysis of the B subunit
of the parasite factor. SMNF-YB contains the conserved HAP-3 homology
domain but the remaining part of the protein was found to be highly
divergent from all other species. We demonstrated by transfections of GAL4
fusion constructs, that mouse NF- YB does not contain activation domains
while the C-terminal part of SMNF-YB has transcriptional activation
potential. On the other hand, the N-terminal parts of SMNF-YA and mouse
NF-YA were shown to mediate transactivation; the integrity of a large 160
amino acid glutamine-rich domain of NF-YA was required for this function
and an adjacent serine- and threonine-rich domain was necessary for full
activity in HepG2, but redundant in other cell types. Transactivation
domains identified in SMNF-YB are also rich in serine and threonine
residues. Our results indicate that serine/threonine-richsequences from
helminth parasites potentiate trans-cription and that such structures have
diverged during evolution within the same transcription factor.
ARTICLES
Conservation and divergence of NF-Y transcriptional activation function
Unite INSERM 167, Institut Pasteur Lille, 1, rue du Professeur Calmette, 59019 Lille, France.
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