Please use this identifier to cite or link to this item:
|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|
Xeroderma pigmentosum complementation group A
|Source:||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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 7, 2017
WEB OF SCIENCETM
checked on Nov 22, 2017
checked on Dec 10, 2017
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.