Please use this identifier to cite or link to this item:
https://doi.org/10.1074/jbc.272.16.10739
DC Field | Value | |
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dc.title | NFI-B3, a novel transcriptional repressor of the nuclear factor I family, is generated by alternative RNA processing | |
dc.contributor.author | Liu, Y. | |
dc.contributor.author | Bernard, H.-U. | |
dc.contributor.author | Apt, D. | |
dc.date.accessioned | 2014-11-28T02:51:54Z | |
dc.date.available | 2014-11-28T02:51:54Z | |
dc.date.issued | 1997-04-18 | |
dc.identifier.citation | Liu, Y.,Bernard, H.-U.,Apt, D. (1997-04-18). NFI-B3, a novel transcriptional repressor of the nuclear factor I family, is generated by alternative RNA processing. Journal of Biological Chemistry 272 (16) : 10739-10745. ScholarBank@NUS Repository. <a href="https://doi.org/10.1074/jbc.272.16.10739" target="_blank">https://doi.org/10.1074/jbc.272.16.10739</a> | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/111987 | |
dc.description.abstract | Nuclear factor I (NFI) proteins constitute a family of sequence-specific transcription factors whose functional diversity is generated through transcription from four different genes (NFI-A, NFI-B, NFI-C, and NFI-X), alternative RNA splicing, and protein heterodimerization. Here we describe a naturally truncated isoform, NFI-B3, which is derived from the human NFI-B gene, in addition to characterizing further human NFI-B1 and NFI-B2, two differentially spliced variants previously isolated from hamster and chicken. Although NFI-B1 and NFI-B2 proteins are translated from an 8.7-kilobase message, the mRNA for NFI-B3 has a size of only 1.8 kilobases. The NFI-B3 message originates from the failure to excise the first intron downstream of the exons encoding the DNA binding domain and subsequent processing of this transcript at an intron-internal polyadenylation signal. The translation product includes the proposed DNA binding and dimerization domain and terminates after translation of two additional 'intron' encoded codons. In SL-2 cells, which are void of endogenous NFI, NFI-B3 by itself had no effect on transcriptional regulation and failed to bind DNA. Coexpression of NFI-B3 with other isoforms of the NFI-B, -C, and -X family, however, led to a strong reduction of transcriptional activation compared with the expression of these factors alone. Gel shift analysis indicated that NFI-B3 disrupts the function of other NFI proteins by reducing their DNA binding activity by heterodimer formation. The efficiency of NFI-B3 heterodimers to bind to DNA correlated with the degree of transcriptional repression. The abundance of NFI-B transcripts varied significantly between different human cell lines and tissues, suggesting a potential involvement of these factors in the complex mechanisms that generate cell type specificity. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.272.16.10739 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1074/jbc.272.16.10739 | |
dc.description.sourcetitle | Journal of Biological Chemistry | |
dc.description.volume | 272 | |
dc.description.issue | 16 | |
dc.description.page | 10739-10745 | |
dc.description.coden | JBCHA | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Staff Publications |
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