Abstract:
:The human ubiquitin-homology domain protein PIC1 interacts with the acute promyelocytic leukemia protein PML, and both proteins form part of the large, nuclear, multiprotein complexes known as PML nuclear bodies. The normal punctate immunohistochemical staining pattern of these complexes is disrupted by viral infection or interferon treatment and in blast cells from patients with acute promyelocytic leukemia. We have characterized the murine homologue of PIC1 and have found that the predicted amino acid sequences of the mouse and human proteins are identical. High levels of Pic1 mRNA were detected in a range of mouse tissues. Pic1 genomic clones were isolated, and the organization of the gene was determined. Two processed Pic1 pseudogenes were also isolated and characterized. Through FISH, the chromosomal localizations of the mouse Pic1 gene and the two pseudogenes were determined. Human PIC1 (HGMW-approved symbol UBL1)-related sequences were isolated from human genomic DNA and were shown to represent processed pseudogenes. The role of PIC1 in a variety of cellular processes is discussed.
journal_name
Genomicsjournal_title
Genomicsauthors
Howe K,Williamson J,Boddy N,Sheer D,Freemont P,Solomon Edoi
10.1006/geno.1997.5091subject
Has Abstractpub_date
1998-01-01 00:00:00pages
92-100issue
1eissn
0888-7543issn
1089-8646pii
S0888-7543(97)95091-6journal_volume
47pub_type
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