Cloning and characterization of the mouse polyamine-modulated factor-1 (mPMF-1) gene: an alternatively spliced homologue of the human transcription factor

• Published in: Biochemical journal 2001-10, Vol.359 (Pt 2), p.387-392
• Main Authors: Wang, Y, Devereux, W, Woster, P M, Casero, Jr, R A
• Format: Article
• Language: English
• Subjects: Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Biogenic Polyamines - metabolism; Biogenic Polyamines - pharmacology; Cell Line; Cloning, Molecular; DNA, Complementary - genetics; DNA-Binding Proteins - metabolism; GA-Binding Protein Transcription Factor; Gene Expression - drug effects; Humans; In Vitro Techniques; Liver - metabolism; Mice; Molecular Sequence Data; Protein Biosynthesis; Protein Structure, Tertiary; Rabbits; RNA, Messenger - genetics; Sequence Homology, Amino Acid; Species Specificity; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; Transcription, Genetic
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/0264-6021:3590387

The natural polyamines and their analogues have been implicated in transcriptional regulation of specific genes. Human polyamine-modulated factor-1 (hPMF-1) was the first polyamine-responsive transcription factor identified. Here the mouse homologue of the hPMF-1 gene is described. Interestingly, the mouse gene (mPMF-1) codes for two alternatively spliced mRNAs. Both of the mouse splice variants, mPMF-1S and mPMF-1L, possess C-terminal coiled-coil domains nearly identical to that found in hPMF-1 and are highly homologous with the human protein. The C-terminal coiled-coil structure is necessary for transcriptional activation. However, the shorter protein, mPMF-1S, does not contain an N-terminal coiled-coil region as do both hPMF-1 and the longer mPMF-1L. mPMF-1L mRNA codes for a protein of 202 amino acids, 37 amino acids longer than the human protein. By contrast, mPMF-1S codes for only 133 amino acids, as a result of two exons being omitted compared with mPMF-1L. Both mouse transcription factors can interact with Nrf-2 (nuclear factor-E2-related factor 2), the normal partner of hPMF-1, substantiating the importance of the C-terminal coiled-coil region responsible for this interaction. Finally, the expression of mPMF-1 is induced when mouse M1 myeloid leukaemia cells are exposed to polyamine analogues, suggesting control similar to that observed for the hPMF-1.