Conservation and divergence of NF-Y transcriptional activation function
Nucleic Acids Research, ISSN: 0305-1048, Vol: 26, Issue: 16, Page: 3800-3805
1998
- 31Citations
- 10Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations31
- Citation Indexes31
- 31
- CrossRef27
- Captures10
- Readers10
- 10
Article Description
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-rich sequences from helminth parasites potentiate transcription and that such structures have diverged during evolution within the same transcription factor.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032529501&origin=inward; http://dx.doi.org/10.1093/nar/26.16.3800; http://www.ncbi.nlm.nih.gov/pubmed/9685499; https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/26.16.3800; https://dx.doi.org/10.1093/nar/26.16.3800; https://academic.oup.com/nar/article/26/16/3800/1021968
Oxford University Press (OUP)
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