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Identification of a novel nuclear speckle‐type protein, SPOP
Author(s) -
Nagai Yasuo,
Kojima Tatsuya,
Muro Yoshinao,
Hachiya Takahisa,
Nishizawa Yuji,
Wakabayashi Takashi,
Hagiwara Masatoshi
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01340-9
Subject(s) - biology , microbiology and biotechnology , complementary dna , peptide sequence , zinc finger , rna splicing , nuclear protein , exon , amino acid , rna , genetics , gene , transcription factor
A novel antigen recognized by serum from a scleroderma patient was identified by expression cloning from the HeLa cell cDNA library. The cloned cDNA encoded a 374‐amino acid protein with a relative molecular mass of 47 000 and a predicted amino acid sequence 62.7% identical to the hypothetical protein of Caenorhabditis elegans , T16H12.5. The deduced amino acid sequence had a typical POZ domain and an unidentified region conserved during evolution. No zinc finger or RNA recognition motifs were found in this clone. The 2 kbp mRNA encoding the novel clone SPOP (speckle‐type POZ protein) was found to be expressed in all human tissues examined. HA‐tagged SPOP, transfected and overexpressed in COS7 cells, exhibited a discrete speckled pattern in the nuclei and was co‐localized with the splicing factor, snRNP B′/B. Deletion analysis revealed that both the POZ domain and the evolutionarily conserved region at the amino‐terminus are required for the nuclear speckled accumulation of SPOP.