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Novelli, G. et al.

Novelli, Mari, Amati, Colosimo, Sangiuolo, Bengala, Conti, Ratti, Bordoni, Pizzuti, Baldini, Crinelli, Pandolfi, Magnani, Dallapiccola,

Structure and expression of the human ubiquitin fusion-degradation gene (UFD1L).

We report the genomic organization, RNA and protein expression patterns of the gene encoding for the human homolog of the yeast ubiquitin fusion-degradation protein-1 (UFD1L). This enzyme is involved in a ubiquitin-dependent proteolytic pathway (UFD), firstly described in yeast. The human UFD1L gene is organized into 12 exons ranging in size from 33 to 161 bp. Sequence analysis of the 5'-flanking region of the gene revealed a high GC content, multiple CCAAT-binding motifs, CREB, CFT, and AP-2 sites. RNA transcripts were detected in all tissues and cell lines examined, including thymus, thymocytes, T- and B-cells, fibroblasts, chorionic villi, and amniocytes. In Western blot, the UFD1L antibody demonstrated the presence of multiple protein isoforms in all the tested tissues. Expression profile and promoter characteristics suggest UFD1L is a housekeeping gene with implications in the pathogenesis of DiGeorge/velo-cardio-facial syndrome, due to 22q11.2 deletions.[1]

References

Structure and expression of the human ubiquitin fusion-degradation gene (UFD1L). Novelli, G., Mari, A., Amati, F., Colosimo, A., Sangiuolo, F., Bengala, M., Conti, E., Ratti, A., Bordoni, R., Pizzuti, A., Baldini, A., Crinelli, R., Pandolfi, F., Magnani, M., Dallapiccola, B. Biochim. Biophys. Acta (1998) [Pubmed]

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