Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.272.16.10739
Title: NFI-B3, a novel transcriptional repressor of the nuclear factor I family, is generated by alternative RNA processing
Authors: Liu, Y. 
Bernard, H.-U. 
Apt, D. 
Issue Date: 18-Apr-1997
Source: 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. https://doi.org/10.1074/jbc.272.16.10739
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.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/111987
ISSN: 00219258
DOI: 10.1074/jbc.272.16.10739
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