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|Title:||The novel human HUEL (C4orf1) protein shares homology with the DNA-binding domain of the XPA DNA repair protein and displays nuclear translocation in a cell cycle-dependent manner||Authors:||Sim, D.L.C.
Xeroderma pigmentosum complementation group A
|Issue Date:||2002||Citation:||Sim, D.L.C., Yeo, W.M., Chow, V.T.K. (2002). The novel human HUEL (C4orf1) protein shares homology with the DNA-binding domain of the XPA DNA repair protein and displays nuclear translocation in a cell cycle-dependent manner. International Journal of Biochemistry and Cell Biology 34 (5) : 487-504. ScholarBank@NUS Repository. https://doi.org/10.1016/S1357-2725(01)00156-X||Abstract:||We have previously isolated and characterized a novel human gene HUEL (C4orf1) that is ubiquitously expressed in a wide range of human fetal, adult tissues and cancer cell lines. HUEL maps to region 4p12-p13 within the short arm of chromosome 4 whose deletion is frequently associated with bladder and other carcinomas. Here we present the genomic organization, sizes and boundaries of exons and introns of HUEL. The GC-rich upstream genomic region and 5′ untranslated region (UTR) together constitute a CpG island, a hallmark of housekeeping genes. The 3250bp HUEL cDNA incorporates a 1704bp ORF that translates into a hydrophilic protein of 568-amino acids (aa), detected as a band of ∼70kDa by Western blotting. We have isolated the murine homolog of HUEL which exhibits 89% nucleotide and 94% amino acid identity to its human counterpart. The HUEL protein shares significant homology with the minimal DNA-binding domain (DNA-BD) of the DNA repair protein encoded by the xeroderma pigmentosum group A (XPA) gene. Other notable features within HUEL include the putative nuclear receptor interaction motif, nuclear localization and export signals, zinc finger, leucine zipper and acidic domains. Mimosine-mediated cell cycle synchronization of PLC/PRF/5 liver cancer cells clearly portrayed translocation of HUEL into the nucleus specifically during the S phase of the cell cycle. Yeast two-hybrid experiments revealed interactions of HUEL with two partner proteins (designated HIPC and HIPB) bearing similarity to a mitotically phosphorylated protein and to reverse transcriptase. Co-immunoprecipitation assays validated the interaction between HUEL and HIPC proteins in mammalian cells. HUEL is likely to be an evolutionarily conserved, housekeeping gene that plays a role intimately linked with cellular replication, DNA synthesis and/or transcriptional regulation. © 2002 Elsevier Science Ltd. All rights reserved.||Source Title:||International Journal of Biochemistry and Cell Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/31295||ISSN:||13572725||DOI:||10.1016/S1357-2725(01)00156-X|
|Appears in Collections:||Staff Publications|
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